2vmv - Revision history

OCA at 15:25, 13 December 2023

2023-12-13T15:25:30Z

← Older revision		Revision as of 15:25, 13 December 2023
Line 3:		Line 3:
	<StructureSection load='2vmv' size='340' side='right'caption='[[2vmv]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='2vmv' size='340' side='right'caption='[[2vmv]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vmv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Atcc_12980 Atcc 12980~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VMV FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vmv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VMV FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=MPD:(4S)~~-~~2-METHYL-2~~,~~4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>~~</td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.7Å</td></tr>
	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>[[1yjy\|1yjy]], [[1kl2\|1kl2]], [[2vib\|2vib]], [[2vgs\|2vgs]], [[1yjz\|1yjz]], [[2vgv\|2vgv]], [[2vgu\|2vgu]], [[1yjs\|1yjs]], [[2vi9\|2vi9]], [[1kl1\|1kl1]], [[2vi8\|2vi8]], [[1kkp\|1kkp]], [[2vgt\|2vgt]], [[2via\|2via]], [[1kkj\|1kkj]], [[2vgw\|2vgw]], [[2vmp\|2vmp]], [[2vmr\|2vmr]], [[2vmu\|2vmu]], [[2vmq\|2vmq]], [[2vms\|2vms]], [[2vmt\|2vmt]], [[2vmw\|2vmw]], [[2vmn\|2vmn]], [[2vmx\|2vmx]], [[2vmo\|2vmo]], [[2vmy\|2vmy]], [[2vmz\|2vmz]]</~~div~~><~~/td></tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1]~~ </~~span~~></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vmv OCA], [https://pdbe.org/2vmv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vmv RCSB], [https://www.ebi.ac.uk/pdbsum/2vmv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vmv ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vmv OCA], [https://pdbe.org/2vmv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vmv RCSB], [https://www.ebi.ac.uk/pdbsum/2vmv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vmv ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/Q7SIB6_GEOSE Q7SIB6_GEOSE]] Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.[HAMAP-Rule:MF_00051]		[https://www.uniprot.org/uniprot/Q7SIB6_GEOSE Q7SIB6_GEOSE] Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.[HAMAP-Rule:MF_00051]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Atcc 12980]]~~		[[Category: Geobacillus stearothermophilus]]
	~~[[Category: Glycine hydroxymethyltransferase~~]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Bhavani, B S]]~~		[[Category: Appaji Rao N]]
	~~[[Category: Bisht, S]]~~		[[Category: Bhavani BS]]
	~~[[Category: Murthy, M R.~~N]]		[[Category: Bisht S]]
	[[Category: ~~Pai, V R~~]]		[[Category: Murthy MRN]]
	[[Category: ~~Rajaram, V]]~~		[[Category: Pai VR]]
	~~[[Category: Rao, N Appaji]]~~		[[Category: Rajaram V]]
	~~[[Category: Savithri, H~~ S]]		[[Category: Savithri HS]]
	[[Category: ~~F351g~~]]
	[[Category: ~~Folate binding~~]]
	[[Category: ~~One-carbon metabolism~~]]
	[[Category: ~~Plp-dependent enzyme]]~~
	~~[[Category: Pyridoxal phosphate]]~~
	~~[[Category: Transferase~~]]

OCA at 11:40, 30 March 2022

2022-03-30T11:40:50Z

← Older revision		Revision as of 11:40, 30 March 2022
Line 3:		Line 3:
	<StructureSection load='2vmv' size='340' side='right'caption='[[2vmv]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='2vmv' size='340' side='right'caption='[[2vmv]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vmv]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VMV OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2VMV FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vmv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VMV FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yjy\|1yjy]], [[1kl2\|1kl2]], [[2vib\|2vib]], [[2vgs\|2vgs]], [[1yjz\|1yjz]], [[2vgv\|2vgv]], [[2vgu\|2vgu]], [[1yjs\|1yjs]], [[2vi9\|2vi9]], [[1kl1\|1kl1]], [[2vi8\|2vi8]], [[1kkp\|1kkp]], [[2vgt\|2vgt]], [[2via\|2via]], [[1kkj\|1kkj]], [[2vgw\|2vgw]], [[2vmp\|2vmp]], [[2vmr\|2vmr]], [[2vmu\|2vmu]], [[2vmq\|2vmq]], [[2vms\|2vms]], [[2vmt\|2vmt]], [[2vmw\|2vmw]], [[2vmn\|2vmn]], [[2vmx\|2vmx]], [[2vmo\|2vmo]], [[2vmy\|2vmy]], [[2vmz\|2vmz]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1yjy\|1yjy]], [[1kl2\|1kl2]], [[2vib\|2vib]], [[2vgs\|2vgs]], [[1yjz\|1yjz]], [[2vgv\|2vgv]], [[2vgu\|2vgu]], [[1yjs\|1yjs]], [[2vi9\|2vi9]], [[1kl1\|1kl1]], [[2vi8\|2vi8]], [[1kkp\|1kkp]], [[2vgt\|2vgt]], [[2via\|2via]], [[1kkj\|1kkj]], [[2vgw\|2vgw]], [[2vmp\|2vmp]], [[2vmr\|2vmr]], [[2vmu\|2vmu]], [[2vmq\|2vmq]], [[2vms\|2vms]], [[2vmt\|2vmt]], [[2vmw\|2vmw]], [[2vmn\|2vmn]], [[2vmx\|2vmx]], [[2vmo\|2vmo]], [[2vmy\|2vmy]], [[2vmz\|2vmz]]</div></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=2vmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vmv OCA], [~~http~~://pdbe.org/2vmv PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2vmv RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2vmv PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2vmv ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vmv OCA], [https://pdbe.org/2vmv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vmv RCSB], [https://www.ebi.ac.uk/pdbsum/2vmv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vmv ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/Q7SIB6_GEOSE Q7SIB6_GEOSE]] Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.[HAMAP-Rule:MF_00051]		[[https://www.uniprot.org/uniprot/Q7SIB6_GEOSE Q7SIB6_GEOSE]] Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.[HAMAP-Rule:MF_00051]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 32:

	==See Also==		==See Also==
	*[[Serine hydroxymethyltransferase\|Serine hydroxymethyltransferase]]		*[[Serine hydroxymethyltransferase 3D structures\|Serine hydroxymethyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:11, 25 June 2020

2020-06-25T08:11:08Z

← Older revision		Revision as of 08:11, 25 June 2020
Line 1:		Line 1:

	==Crystal structure of F351GbsSHMT internal aldimine==		==Crystal structure of F351GbsSHMT internal aldimine==
	<StructureSection load='2vmv' size='340' side='right' caption='[[2vmv]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='2vmv' size='340' side='right'caption='[[2vmv]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vmv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VMV OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2VMV FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vmv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VMV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VMV FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yjy\|1yjy]], [[1kl2\|1kl2]], [[2vib\|2vib]], [[2vgs\|2vgs]], [[1yjz\|1yjz]], [[2vgv\|2vgv]], [[2vgu\|2vgu]], [[1yjs\|1yjs]], [[2vi9\|2vi9]], [[1kl1\|1kl1]], [[2vi8\|2vi8]], [[1kkp\|1kkp]], [[2vgt\|2vgt]], [[2via\|2via]], [[1kkj\|1kkj]], [[2vgw\|2vgw]], [[2vmp\|2vmp]], [[2vmr\|2vmr]], [[2vmu\|2vmu]], [[2vmq\|2vmq]], [[2vms\|2vms]], [[2vmt\|2vmt]], [[2vmw\|2vmw]], [[2vmn\|2vmn]], [[2vmx\|2vmx]], [[2vmo\|2vmo]], [[2vmy\|2vmy]], [[2vmz\|2vmz]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yjy\|1yjy]], [[1kl2\|1kl2]], [[2vib\|2vib]], [[2vgs\|2vgs]], [[1yjz\|1yjz]], [[2vgv\|2vgv]], [[2vgu\|2vgu]], [[1yjs\|1yjs]], [[2vi9\|2vi9]], [[1kl1\|1kl1]], [[2vi8\|2vi8]], [[1kkp\|1kkp]], [[2vgt\|2vgt]], [[2via\|2via]], [[1kkj\|1kkj]], [[2vgw\|2vgw]], [[2vmp\|2vmp]], [[2vmr\|2vmr]], [[2vmu\|2vmu]], [[2vmq\|2vmq]], [[2vms\|2vms]], [[2vmt\|2vmt]], [[2vmw\|2vmw]], [[2vmn\|2vmn]], [[2vmx\|2vmx]], [[2vmo\|2vmo]], [[2vmy\|2vmy]], [[2vmz\|2vmz]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2vmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vmv OCA], [http://pdbe.org/2vmv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vmv RCSB], [http://www.ebi.ac.uk/pdbsum/2vmv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vmv ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2vmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vmv OCA], [http://pdbe.org/2vmv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vmv RCSB], [http://www.ebi.ac.uk/pdbsum/2vmv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vmv ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 39:		Line 39:
	[[Category: Atcc 12980]]		[[Category: Atcc 12980]]
	[[Category: Glycine hydroxymethyltransferase]]		[[Category: Glycine hydroxymethyltransferase]]
			[[Category: Large Structures]]
	[[Category: Bhavani, B S]]		[[Category: Bhavani, B S]]
	[[Category: Bisht, S]]		[[Category: Bisht, S]]

OCA at 20:57, 19 September 2018

2018-09-19T20:57:05Z

← Older revision		Revision as of 20:57, 19 September 2018
Line 1:		Line 1:
	==~~CRYSTAL STRUCTURE OF F351GBSSHMT INTERNAL ALDIMINE~~==
			==Crystal structure of F351GbsSHMT internal aldimine==
	<StructureSection load='2vmv' size='340' side='right' caption='[[2vmv]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='2vmv' size='340' side='right' caption='[[2vmv]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yjy\|1yjy]], [[1kl2\|1kl2]], [[2vib\|2vib]], [[2vgs\|2vgs]], [[1yjz\|1yjz]], [[2vgv\|2vgv]], [[2vgu\|2vgu]], [[1yjs\|1yjs]], [[2vi9\|2vi9]], [[1kl1\|1kl1]], [[2vi8\|2vi8]], [[1kkp\|1kkp]], [[2vgt\|2vgt]], [[2via\|2via]], [[1kkj\|1kkj]], [[2vgw\|2vgw]], [[2vmp\|2vmp]], [[2vmr\|2vmr]], [[2vmu\|2vmu]], [[2vmq\|2vmq]], [[2vms\|2vms]], [[2vmt\|2vmt]], [[2vmw\|2vmw]], [[2vmn\|2vmn]], [[2vmx\|2vmx]], [[2vmo\|2vmo]], [[2vmy\|2vmy]], [[2vmz\|2vmz]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yjy\|1yjy]], [[1kl2\|1kl2]], [[2vib\|2vib]], [[2vgs\|2vgs]], [[1yjz\|1yjz]], [[2vgv\|2vgv]], [[2vgu\|2vgu]], [[1yjs\|1yjs]], [[2vi9\|2vi9]], [[1kl1\|1kl1]], [[2vi8\|2vi8]], [[1kkp\|1kkp]], [[2vgt\|2vgt]], [[2via\|2via]], [[1kkj\|1kkj]], [[2vgw\|2vgw]], [[2vmp\|2vmp]], [[2vmr\|2vmr]], [[2vmu\|2vmu]], [[2vmq\|2vmq]], [[2vms\|2vms]], [[2vmt\|2vmt]], [[2vmw\|2vmw]], [[2vmn\|2vmn]], [[2vmx\|2vmx]], [[2vmo\|2vmo]], [[2vmy\|2vmy]], [[2vmz\|2vmz]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vmv OCA], [http://pdbe.org/2vmv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vmv RCSB], [http://www.ebi.ac.uk/pdbsum/2vmv PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vmv OCA], [http://pdbe.org/2vmv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vmv RCSB], [http://www.ebi.ac.uk/pdbsum/2vmv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vmv ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vm/2vmv_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vm/2vmv_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 13:24, 9 February 2016

2016-02-09T13:24:04Z

← Older revision		Revision as of 13:24, 9 February 2016
Line 2:		Line 2:
	<StructureSection load='2vmv' size='340' side='right' caption='[[2vmv]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='2vmv' size='340' side='right' caption='[[2vmv]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vmv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Geobacillus_stearothermophilus Geobacillus stearothermophilus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VMV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VMV FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vmv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VMV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VMV FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yjy\|1yjy]], [[1kl2\|1kl2]], [[2vib\|2vib]], [[2vgs\|2vgs]], [[1yjz\|1yjz]], [[2vgv\|2vgv]], [[2vgu\|2vgu]], [[1yjs\|1yjs]], [[2vi9\|2vi9]], [[1kl1\|1kl1]], [[2vi8\|2vi8]], [[1kkp\|1kkp]], [[2vgt\|2vgt]], [[2via\|2via]], [[1kkj\|1kkj]], [[2vgw\|2vgw]], [[2vmp\|2vmp]], [[2vmr\|2vmr]], [[2vmu\|2vmu]], [[2vmq\|2vmq]], [[2vms\|2vms]], [[2vmt\|2vmt]], [[2vmw\|2vmw]], [[2vmn\|2vmn]], [[2vmx\|2vmx]], [[2vmo\|2vmo]], [[2vmy\|2vmy]], [[2vmz\|2vmz]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yjy\|1yjy]], [[1kl2\|1kl2]], [[2vib\|2vib]], [[2vgs\|2vgs]], [[1yjz\|1yjz]], [[2vgv\|2vgv]], [[2vgu\|2vgu]], [[1yjs\|1yjs]], [[2vi9\|2vi9]], [[1kl1\|1kl1]], [[2vi8\|2vi8]], [[1kkp\|1kkp]], [[2vgt\|2vgt]], [[2via\|2via]], [[1kkj\|1kkj]], [[2vgw\|2vgw]], [[2vmp\|2vmp]], [[2vmr\|2vmr]], [[2vmu\|2vmu]], [[2vmq\|2vmq]], [[2vms\|2vms]], [[2vmt\|2vmt]], [[2vmw\|2vmw]], [[2vmn\|2vmn]], [[2vmx\|2vmx]], [[2vmo\|2vmo]], [[2vmy\|2vmy]], [[2vmz\|2vmz]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vmv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vmv RCSB], [http://www.ebi.ac.uk/pdbsum/2vmv PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vmv OCA], [http://pdbe.org/2vmv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vmv RCSB], [http://www.ebi.ac.uk/pdbsum/2vmv PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/~~Q7SIB6_BACST Q7SIB6_BACST~~]] Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism ~~(By similarity)~~.[HAMAP-Rule:MF_00051~~] Interconversion of serine and glycine (By similarity).[RuleBase:RU000585~~]		[[http://www.uniprot.org/uniprot/Q7SIB6_GEOSE Q7SIB6_GEOSE]] Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.[HAMAP-Rule:MF_00051]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 18:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vmv ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		Line 28:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 2vmv" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Geobacillus stearothermophilus~~]]		[[Category: Atcc 12980]]
	[[Category: Glycine hydroxymethyltransferase]]		[[Category: Glycine hydroxymethyltransferase]]
	[[Category: Bhavani, B S]]		[[Category: Bhavani, B S]]

OCA at 07:04, 25 December 2014

2014-12-25T07:04:43Z

← Older revision		Revision as of 07:04, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vmv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VMV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VMV FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vmv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VMV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VMV FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yjy\|1yjy]], [[1kl2\|1kl2]], [[2vib\|2vib]], [[2vgs\|2vgs]], [[1yjz\|1yjz]], [[2vgv\|2vgv]], [[2vgu\|2vgu]], [[1yjs\|1yjs]], [[2vi9\|2vi9]], [[1kl1\|1kl1]], [[2vi8\|2vi8]], [[1kkp\|1kkp]], [[2vgt\|2vgt]], [[2via\|2via]], [[1kkj\|1kkj]], [[2vgw\|2vgw]], [[2vmp\|2vmp]], [[2vmr\|2vmr]], [[2vmu\|2vmu]], [[2vmq\|2vmq]], [[2vms\|2vms]], [[2vmt\|2vmt]], [[2vmw\|2vmw]], [[2vmn\|2vmn]], [[2vmx\|2vmx]], [[2vmo\|2vmo]], [[2vmy\|2vmy]], [[2vmz\|2vmz]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yjy\|1yjy]], [[1kl2\|1kl2]], [[2vib\|2vib]], [[2vgs\|2vgs]], [[1yjz\|1yjz]], [[2vgv\|2vgv]], [[2vgu\|2vgu]], [[1yjs\|1yjs]], [[2vi9\|2vi9]], [[1kl1\|1kl1]], [[2vi8\|2vi8]], [[1kkp\|1kkp]], [[2vgt\|2vgt]], [[2via\|2via]], [[1kkj\|1kkj]], [[2vgw\|2vgw]], [[2vmp\|2vmp]], [[2vmr\|2vmr]], [[2vmu\|2vmu]], [[2vmq\|2vmq]], [[2vms\|2vms]], [[2vmt\|2vmt]], [[2vmw\|2vmw]], [[2vmn\|2vmn]], [[2vmx\|2vmx]], [[2vmo\|2vmo]], [[2vmy\|2vmy]], [[2vmz\|2vmz]]</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1] </span></td></tr>
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vmv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vmv RCSB], [http://www.ebi.ac.uk/pdbsum/2vmv PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vmv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vmv RCSB], [http://www.ebi.ac.uk/pdbsum/2vmv PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/Q7SIB6_BACST Q7SIB6_BACST]] Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism (By similarity).[HAMAP-Rule:MF_00051] Interconversion of serine and glycine (By similarity).[RuleBase:RU000585]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 37:
	[[Category: Geobacillus stearothermophilus]]		[[Category: Geobacillus stearothermophilus]]
	[[Category: Glycine hydroxymethyltransferase]]		[[Category: Glycine hydroxymethyltransferase]]
	[[Category: Bhavani, B S.]]		[[Category: Bhavani, B S]]
	[[Category: Bisht, S.]]		[[Category: Bisht, S]]
	[[Category: Murthy, M R.N.]]		[[Category: Murthy, M R.N]]
	[[Category: Pai, V R.]]		[[Category: Pai, V R]]
	[[Category: Rajaram, V.]]		[[Category: Rajaram, V]]
	[[Category: Rao, N Appaji.]]		[[Category: Rao, N Appaji]]
	[[Category: Savithri, H S.]]		[[Category: Savithri, H S]]
	[[Category: F351g]]		[[Category: F351g]]
	[[Category: Folate binding]]		[[Category: Folate binding]]

OCA at 01:29, 1 October 2014

2014-10-01T01:29:21Z

← Older revision		Revision as of 01:29, 1 October 2014
Line 1:		Line 1:
	[[Image:~~2vmv~~.~~png~~\|~~left~~\|~~200px~~]]		==CRYSTAL STRUCTURE OF F351GBSSHMT INTERNAL ALDIMINE==
			<StructureSection load='2vmv' size='340' side='right' caption='[[2vmv]], [[Resolution\|resolution]] 1.70Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[2vmv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VMV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VMV FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene><br>
			<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yjy\|1yjy]], [[1kl2\|1kl2]], [[2vib\|2vib]], [[2vgs\|2vgs]], [[1yjz\|1yjz]], [[2vgv\|2vgv]], [[2vgu\|2vgu]], [[1yjs\|1yjs]], [[2vi9\|2vi9]], [[1kl1\|1kl1]], [[2vi8\|2vi8]], [[1kkp\|1kkp]], [[2vgt\|2vgt]], [[2via\|2via]], [[1kkj\|1kkj]], [[2vgw\|2vgw]], [[2vmp\|2vmp]], [[2vmr\|2vmr]], [[2vmu\|2vmu]], [[2vmq\|2vmq]], [[2vms\|2vms]], [[2vmt\|2vmt]], [[2vmw\|2vmw]], [[2vmn\|2vmn]], [[2vmx\|2vmx]], [[2vmo\|2vmo]], [[2vmy\|2vmy]], [[2vmz\|2vmz]]</td></tr>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1] </span></td></tr>
			<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vmv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vmv RCSB], [http://www.ebi.ac.uk/pdbsum/2vmv PDBsum]</span></td></tr>
			<table>
			== Evolutionary Conservation ==
			[[Image:Consurf_key_small.gif\|200px\|right]]
			Check<jmol>
			<jmolCheckbox>
			<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vm/2vmv_consurf.spt"</scriptWhenChecked>
			<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
			<text>to colour the structure by Evolutionary Conservation</text>
			</jmolCheckbox>
			</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
			<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			SHMT (serine hydoxymethyltransferase), a type I pyridoxal 5'-phosphate-dependent enzyme, catalyses the conversion of L-serine and THF (tetrahydrofolate) into glycine and 5,10-methylene THF. SHMT also catalyses several THF-independent side reactions such as cleavage of beta-hydroxy amino acids, transamination, racemization and decarboxylation. In the present study, the residues Asn(341), Tyr(60) and Phe(351), which are likely to influence THF binding, were mutated to alanine, alanine and glycine respectively, to elucidate the role of these residues in THF-dependent and -independent reactions catalysed by SHMT. The N341A and Y60A bsSHMT (Bacillus stearothermophilus SHMT) mutants were inactive for the THF-dependent activity, while the mutations had no effect on THF-independent activity. However, mutation of Phe(351) to glycine did not have any effect on either of the activities. The crystal structures of the glycine binary complexes of the mutants showed that N341A bsSHMT forms an external aldimine as in bsSHMT, whereas Y60A and F351G bsSHMTs exist as a mixture of internal/external aldimine and gem-diamine forms. Crystal structures of all of the three mutants obtained in the presence of L-allo-threonine were similar to the respective glycine binary complexes. The structure of the ternary complex of F351G bsSHMT with glycine and FTHF (5-formyl THF) showed that the monoglutamate side chain of FTHF is ordered in both the subunits of the asymmetric unit, unlike in the wild-type bsSHMT. The present studies demonstrate that the residues Asn(341) and Tyr(60) are pivotal for the binding of THF/FTHF, whereas Phe(351) is responsible for the asymmetric binding of FTHF in the two subunits of the dimer.

	~~{{STRUCTURE_2vmv\| PDB=2vmv \| SCENE= }}~~		Structural and functional studies of Bacillus stearothermophilus serine hydroxymethyltransferase: the role of Asn(341), Tyr(60) and Phe(351) in tetrahydrofolate binding.,Pai VR, Rajaram V, Bisht S, Bhavani BS, Rao NA, Murthy MR, Savithri HS Biochem J. 2009 Mar 15;418(3):635-42. PMID:19046138<ref>PMID:19046138</ref>

	~~===CRYSTAL STRUCTURE OF F351GBSSHMT INTERNAL ALDIMINE===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

	~~{{ABSTRACT_PUBMED_19046138}}~~		==See Also==
			*[[Serine hydroxymethyltransferase\|Serine hydroxymethyltransferase]]
	==~~About this Structure~~==		== References ==
	[[~~2vmv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus~~]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VMV OCA~~].		<references/>
			__TOC__
	==~~Reference~~==		</StructureSection>
	<~~ref group="xtra">PMID:019046138<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Geobacillus stearothermophilus]]		[[Category: Geobacillus stearothermophilus]]
	[[Category: Glycine hydroxymethyltransferase]]		[[Category: Glycine hydroxymethyltransferase]]

OCA at 13:22, 30 January 2013

2013-01-30T13:22:58Z

← Older revision		Revision as of 13:22, 30 January 2013
Line 1:		Line 1:
	[[Image:2vmv.png\|left\|200px]]		[[Image:2vmv.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_2vmv", creates the "Structure Box" on the page.~~
	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~
	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~
	~~or leave the SCENE parameter empty for the default display.~~
	~~-->~~
	{{STRUCTURE_2vmv\| PDB=2vmv \| SCENE= }}		{{STRUCTURE_2vmv\| PDB=2vmv \| SCENE= }}

	===CRYSTAL STRUCTURE OF F351GBSSHMT INTERNAL ALDIMINE===		===CRYSTAL STRUCTURE OF F351GBSSHMT INTERNAL ALDIMINE===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_19046138}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 19046138 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_19046138}}		{{ABSTRACT_PUBMED_19046138}}

Line 22:		Line 11:

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~19046138~~</ref><references group="xtra"/>		<ref group="xtra">PMID:019046138</ref><references group="xtra"/>
	[[Category: Geobacillus stearothermophilus]]		[[Category: Geobacillus stearothermophilus]]
	[[Category: Glycine hydroxymethyltransferase]]		[[Category: Glycine hydroxymethyltransferase]]
Line 32:		Line 21:
	[[Category: Rao, N Appaji.]]		[[Category: Rao, N Appaji.]]
	[[Category: Savithri, H S.]]		[[Category: Savithri, H S.]]
			[[Category: F351g]]
			[[Category: Folate binding]]
			[[Category: One-carbon metabolism]]
			[[Category: Plp-dependent enzyme]]
			[[Category: Pyridoxal phosphate]]
			[[Category: Transferase]]

OCA: Protected "2vmv" [edit=sysop:move=sysop]

2011-03-23T06:29:20Z

Protected "2vmv" [edit=sysop:move=sysop]

← Older revision	Revision as of 06:29, 23 March 2011
(No difference)

OCA at 06:29, 23 March 2011

2011-03-23T06:29:18Z

← Older revision		Revision as of 06:29, 23 March 2011
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	~~{{Seed}}~~		[[Image:2vmv.png\|left\|200px]]
	[[Image:2vmv.~~jpg~~\|left\|200px]]

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	==About this Structure==		==About this Structure==
	~~2VMV~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VMV OCA].		[[2vmv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VMV OCA].

	==Reference==		==Reference==
	Structural and functional studies of Bacillus stearothermophilus serine hydroxymethyltransferase: the role of N341, Y60 and F351 in tetrahydrofolate binding., Pai VR, Rajaram V, Bisht S, Bhavani BS, Rao NA, Murthy MR, Savithri HS, Biochem J. 2008 Dec 1. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/19046138 19046138]~~		<ref group="xtra">PMID:19046138</ref><references group="xtra"/>
	[[Category: Geobacillus stearothermophilus]]		[[Category: Geobacillus stearothermophilus]]
	[[Category: Glycine hydroxymethyltransferase]]		[[Category: Glycine hydroxymethyltransferase]]
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	[[Category: Rao, N Appaji.]]		[[Category: Rao, N Appaji.]]
	[[Category: Savithri, H S.]]		[[Category: Savithri, H S.]]
	~~[[Category: F351g]]~~
	~~[[Category: Folate binding]]~~
	~~[[Category: One-carbon metabolism]]~~
	~~[[Category: Plp-dependent enzyme]]~~
	~~[[Category: Pyridoxal phosphate]]~~
	~~[[Category: Serine hydroxymethyltransferase]]~~
	~~[[Category: Shmt]]~~
	~~[[Category: Transferase]]~~

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 17 13:27:49 2008''~~