3typ - Revision history

OCA at 10:15, 1 March 2024

2024-03-01T10:15:48Z

← Older revision		Revision as of 10:15, 1 March 2024
Line 3:		Line 3:
	<StructureSection load='3typ' size='340' side='right'caption='[[3typ]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='3typ' size='340' side='right'caption='[[3typ]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3typ]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"bacterium_nitrosomonas"_lehmann_and_neumann_1899 "bacterium nitrosomonas" lehmann and neumann 1899~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TYP FirstGlance]. <br>		<table><tr><td colspan='2'>[[3typ]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nitrosomonas_europaea Nitrosomonas europaea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TYP FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=EDO:1,2~~-~~ETHANEDIOL'>EDO</scene>~~, ~~<scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.9Å</td></tr>
	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[2fbl\|2fbl]]~~</~~div~~><~~/td></tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></~~td><td class="sblockDat"~~>~~NE1496 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=915 "Bacterium nitrosomonas" Lehmann and Neumann 1899])~~</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=3typ FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3typ OCA], [https://pdbe.org/3typ PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3typ RCSB], [https://www.ebi.ac.uk/pdbsum/3typ PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3typ 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=3typ FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3typ OCA], [https://pdbe.org/3typ PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3typ RCSB], [https://www.ebi.ac.uk/pdbsum/3typ PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3typ ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/3PASE_NITEU 3PASE_NITEU]] Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside-linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi). The enzyme has a strong preference for linear PPPi compared with cyclic PPPi (cyclic trimetaphosphate) and to the linear P4. The longer chains polyphosphate are not hydrolyzed. It has only a slight thiamine triphosphatase (ThTPase) activity. Nucleoside triphosphatase activity is negligible in the presence of magnesium, but a small activity is observed in the presence of manganese, in particular with GTP.<ref>PMID:21840996</ref>		[https://www.uniprot.org/uniprot/3PASE_NITEU 3PASE_NITEU] Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside-linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi). The enzyme has a strong preference for linear PPPi compared with cyclic PPPi (cyclic trimetaphosphate) and to the linear P4. The longer chains polyphosphate are not hydrolyzed. It has only a slight thiamine triphosphatase (ThTPase) activity. Nucleoside triphosphatase activity is negligible in the presence of magnesium, but a small activity is observed in the presence of manganese, in particular with GTP.<ref>PMID:21840996</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	The CYTH superfamily of proteins is named after its two founding members, the CyaB adenylyl cyclase from Aeromonas hydrophila and the human 25-kDa thiamine triphosphatase. Because these proteins often form a closed beta-barrel, they are also referred to as triphosphate tunnel metalloenzymes (TTM). Functionally, they are characterized by their ability to bind triphosphorylated substrates and divalent metal ions. These proteins exist in most organisms and catalyze different reactions depending on their origin. Here we investigate structural and catalytic properties of the recombinant TTM protein from Nitrosomonas europaea (NeuTTM), a 19-kDa protein. Crystallographic data show that it crystallizes as a dimer and that, in contrast to other TTM proteins, it has an open beta-barrel structure. We demonstrate that NeuTTM is a highly specific inorganic triphosphatase, hydrolyzing tripolyphosphate (PPP(i)) with high catalytic efficiency in the presence of Mg(2+). These data are supported by native mass spectrometry analysis showing that the enzyme binds PPP(i) (and Mg-PPP(i)) with high affinity (K(d) < 1.5 mum), whereas it has a low affinity for ATP or thiamine triphosphate. In contrast to Aeromonas and Yersinia CyaB proteins, NeuTTM has no adenylyl cyclase activity, but it shares several properties with other enzymes of the CYTH superfamily, e.g. heat stability, alkaline pH optimum, and inhibition by Ca(2+) and Zn(2+) ions. We suggest a catalytic mechanism involving a catalytic dyad formed by Lys-52 and Tyr-28. The present data provide the first characterization of a new type of phosphohydrolase (unrelated to pyrophosphatases or exopolyphosphatases), able to hydrolyze inorganic triphosphate with high specificity.

	A specific inorganic triphosphatase from Nitrosomonas europaea: structure and catalytic mechanism.,Delvaux D, Murty MR, Gabelica V, Lakaye B, Lunin VV, Skarina T, Onopriyenko O, Kohn G, Wins P, De Pauw E, Bettendorff L J Biol Chem. 2011 Sep 30;286(39):34023-35. Epub 2011 Aug 12. PMID:21840996<ref>PMID:21840996</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 3typ" style="background-color:#fffaf0;"></div~~>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: Bacterium nitrosomonas lehmann and neumann 1899]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Binkowski~~, T A~~]]		[[Category: Nitrosomonas europaea]]
	[[Category: Edwards~~, A M~~]]		[[Category: Binkowski TA]]
	[[Category: Joachimiak, A]]		[[Category: Edwards AM]]
	[[Category: Lunin~~, V V~~]]		[[Category: Joachimiak A]]
	[[Category: Onopriyenko, O]]		[[Category: Lunin VV]]
	[[Category: Savchenko, A]]		[[Category: Onopriyenko O]]
	[[Category: Skarina, T]]		[[Category: Savchenko A]]
	~~[[Category: Hydrolase]]~~		[[Category: Skarina T]]
	~~[[Category: Inorganic triphosphatase~~]]

OCA at 05:50, 13 July 2022

2022-07-13T05:50:46Z

← Older revision		Revision as of 05:50, 13 July 2022
Line 1:		Line 1:

	==The crystal structure of the inorganic triphosphatase NE1496==		==The crystal structure of the inorganic triphosphatase NE1496==
	<StructureSection load='3typ' size='340' side='right' caption='[[3typ]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='3typ' size='340' side='right'caption='[[3typ]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3typ]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"bacterium_nitrosomonas"_lehmann_and_neumann_1899 "bacterium nitrosomonas" lehmann and neumann 1899]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TYP OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3TYP FirstGlance]. <br>		<table><tr><td colspan='2'>[[3typ]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_nitrosomonas"_lehmann_and_neumann_1899 "bacterium nitrosomonas" lehmann and neumann 1899]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TYP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fbl\|2fbl]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2fbl\|2fbl]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NE1496 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=915 "Bacterium nitrosomonas" Lehmann and Neumann 1899])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NE1496 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=915 "Bacterium nitrosomonas" Lehmann and Neumann 1899])</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=3typ FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3typ OCA], [~~http~~://pdbe.org/3typ PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3typ RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3typ PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3typ 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=3typ FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3typ OCA], [https://pdbe.org/3typ PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3typ RCSB], [https://www.ebi.ac.uk/pdbsum/3typ PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3typ ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/3PASE_NITEU 3PASE_NITEU]] Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside-linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi). The enzyme has a strong preference for linear PPPi compared with cyclic PPPi (cyclic trimetaphosphate) and to the linear P4. The longer chains polyphosphate are not hydrolyzed. It has only a slight thiamine triphosphatase (ThTPase) activity. Nucleoside triphosphatase activity is negligible in the presence of magnesium, but a small activity is observed in the presence of manganese, in particular with GTP.<ref>PMID:21840996</ref>		[[https://www.uniprot.org/uniprot/3PASE_NITEU 3PASE_NITEU]] Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside-linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi). The enzyme has a strong preference for linear PPPi compared with cyclic PPPi (cyclic trimetaphosphate) and to the linear P4. The longer chains polyphosphate are not hydrolyzed. It has only a slight thiamine triphosphatase (ThTPase) activity. Nucleoside triphosphatase activity is negligible in the presence of magnesium, but a small activity is observed in the presence of manganese, in particular with GTP.<ref>PMID:21840996</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Bacterium nitrosomonas lehmann and neumann 1899]]		[[Category: Bacterium nitrosomonas lehmann and neumann 1899]]
			[[Category: Large Structures]]
	[[Category: Binkowski, T A]]		[[Category: Binkowski, T A]]
	[[Category: Edwards, A M]]		[[Category: Edwards, A M]]

OCA at 11:22, 4 August 2016

2016-08-04T11:22:09Z

← Older revision		Revision as of 11:22, 4 August 2016
Line 1:		Line 1:

	==The crystal structure of the inorganic triphosphatase NE1496==		==The crystal structure of the inorganic triphosphatase NE1496==
	<StructureSection load='3typ' size='340' side='right' caption='[[3typ]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='3typ' size='340' side='right' caption='[[3typ]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3typ]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Nitrosomonas_europaea Nitrosomonas europaea~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TYP FirstGlance]. <br>		<table><tr><td colspan='2'>[[3typ]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_nitrosomonas"_lehmann_and_neumann_1899 "bacterium nitrosomonas" lehmann and neumann 1899]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TYP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fbl\|2fbl]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fbl\|2fbl]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NE1496 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=915 ~~Nitrosomonas europaea~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NE1496 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=915 "Bacterium nitrosomonas" Lehmann and Neumann 1899])</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=3typ FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3typ OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3typ RCSB], [http://www.ebi.ac.uk/pdbsum/3typ 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=3typ FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3typ OCA], [http://pdbe.org/3typ PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3typ RCSB], [http://www.ebi.ac.uk/pdbsum/3typ PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3typ ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/~~Q82UI9_NITEU Q82UI9_NITEU~~]] Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside-linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi). The enzyme has a strong preference for linear PPPi compared with cyclic PPPi (cyclic trimetaphosphate) and to the linear P4. The longer chains polyphosphate are not hydrolyzed. It has only a slight thiamine triphosphatase (ThTPase) activity. Nucleoside triphosphatase activity is negligible in the presence of magnesium, but a small activity is observed in the presence of manganese, in particular with GTP.		[[http://www.uniprot.org/uniprot/3PASE_NITEU 3PASE_NITEU]] Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside-linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi). The enzyme has a strong preference for linear PPPi compared with cyclic PPPi (cyclic trimetaphosphate) and to the linear P4. The longer chains polyphosphate are not hydrolyzed. It has only a slight thiamine triphosphatase (ThTPase) activity. Nucleoside triphosphatase activity is negligible in the presence of magnesium, but a small activity is observed in the presence of manganese, in particular with GTP.<ref>PMID:21840996</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 18:		Line 19:
	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 3typ" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Nitrosomonas europaea~~]]		[[Category: Bacterium nitrosomonas lehmann and neumann 1899]]
	[[Category: Binkowski, T A]]		[[Category: Binkowski, T A]]
	[[Category: Edwards, A M]]		[[Category: Edwards, A M]]

OCA at 08:48, 25 December 2014

2014-12-25T08:48:22Z

← Older revision		Revision as of 08:48, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3typ]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Nitrosomonas_europaea Nitrosomonas europaea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TYP FirstGlance]. <br>		<table><tr><td colspan='2'>[[3typ]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Nitrosomonas_europaea Nitrosomonas europaea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TYP FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fbl\|2fbl]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fbl\|2fbl]]</td></tr>
	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NE1496 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=915 Nitrosomonas europaea])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NE1496 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=915 Nitrosomonas europaea])</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=3typ FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3typ OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3typ RCSB], [http://www.ebi.ac.uk/pdbsum/3typ 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=3typ FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3typ OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3typ RCSB], [http://www.ebi.ac.uk/pdbsum/3typ PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/Q82UI9_NITEU Q82UI9_NITEU]] Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside-linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi). The enzyme has a strong preference for linear PPPi compared with cyclic PPPi (cyclic trimetaphosphate) and to the linear P4. The longer chains polyphosphate are not hydrolyzed. It has only a slight thiamine triphosphatase (ThTPase) activity. Nucleoside triphosphatase activity is negligible in the presence of magnesium, but a small activity is observed in the presence of manganese, in particular with GTP.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 14:		Line 16:
	A specific inorganic triphosphatase from Nitrosomonas europaea: structure and catalytic mechanism.,Delvaux D, Murty MR, Gabelica V, Lakaye B, Lunin VV, Skarina T, Onopriyenko O, Kohn G, Wins P, De Pauw E, Bettendorff L J Biol Chem. 2011 Sep 30;286(39):34023-35. Epub 2011 Aug 12. PMID:21840996<ref>PMID:21840996</ref>		A specific inorganic triphosphatase from Nitrosomonas europaea: structure and catalytic mechanism.,Delvaux D, Murty MR, Gabelica V, Lakaye B, Lunin VV, Skarina T, Onopriyenko O, Kohn G, Wins P, De Pauw E, Bettendorff L J Biol Chem. 2011 Sep 30;286(39):34023-35. Epub 2011 Aug 12. PMID:21840996<ref>PMID:21840996</ref>

	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>
	== References ==		== References ==
Line 21:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Nitrosomonas europaea]]		[[Category: Nitrosomonas europaea]]
	[[Category: Binkowski, T A.]]		[[Category: Binkowski, T A]]
	[[Category: Edwards, A M.]]		[[Category: Edwards, A M]]
	[[Category: Joachimiak, A.]]		[[Category: Joachimiak, A]]
	[[Category: Lunin, V V.]]		[[Category: Lunin, V V]]
	[[Category: Onopriyenko, O.]]		[[Category: Onopriyenko, O]]
	[[Category: Savchenko, A.]]		[[Category: Savchenko, A]]
	[[Category: Skarina, T.]]		[[Category: Skarina, T]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Inorganic triphosphatase]]		[[Category: Inorganic triphosphatase]]

OCA at 06:10, 5 June 2014

2014-06-05T06:10:31Z

← Older revision		Revision as of 06:10, 5 June 2014
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	[[~~Image~~:~~3typ~~.~~png~~\|~~left~~\|~~200px~~]]		==The crystal structure of the inorganic triphosphatase NE1496==
			<StructureSection load='3typ' size='340' side='right' caption='[[3typ]], [[Resolution\|resolution]] 1.90Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[3typ]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Nitrosomonas_europaea Nitrosomonas europaea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TYP FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>
			<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fbl\|2fbl]]</td></tr>
			<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NE1496 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=915 Nitrosomonas europaea])</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=3typ FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3typ OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3typ RCSB], [http://www.ebi.ac.uk/pdbsum/3typ PDBsum]</span></td></tr>
			<table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The CYTH superfamily of proteins is named after its two founding members, the CyaB adenylyl cyclase from Aeromonas hydrophila and the human 25-kDa thiamine triphosphatase. Because these proteins often form a closed beta-barrel, they are also referred to as triphosphate tunnel metalloenzymes (TTM). Functionally, they are characterized by their ability to bind triphosphorylated substrates and divalent metal ions. These proteins exist in most organisms and catalyze different reactions depending on their origin. Here we investigate structural and catalytic properties of the recombinant TTM protein from Nitrosomonas europaea (NeuTTM), a 19-kDa protein. Crystallographic data show that it crystallizes as a dimer and that, in contrast to other TTM proteins, it has an open beta-barrel structure. We demonstrate that NeuTTM is a highly specific inorganic triphosphatase, hydrolyzing tripolyphosphate (PPP(i)) with high catalytic efficiency in the presence of Mg(2+). These data are supported by native mass spectrometry analysis showing that the enzyme binds PPP(i) (and Mg-PPP(i)) with high affinity (K(d) < 1.5 mum), whereas it has a low affinity for ATP or thiamine triphosphate. In contrast to Aeromonas and Yersinia CyaB proteins, NeuTTM has no adenylyl cyclase activity, but it shares several properties with other enzymes of the CYTH superfamily, e.g. heat stability, alkaline pH optimum, and inhibition by Ca(2+) and Zn(2+) ions. We suggest a catalytic mechanism involving a catalytic dyad formed by Lys-52 and Tyr-28. The present data provide the first characterization of a new type of phosphohydrolase (unrelated to pyrophosphatases or exopolyphosphatases), able to hydrolyze inorganic triphosphate with high specificity.

	~~{{STRUCTURE_3typ\| PDB=3typ \| SCENE= }}~~		A specific inorganic triphosphatase from Nitrosomonas europaea: structure and catalytic mechanism.,Delvaux D, Murty MR, Gabelica V, Lakaye B, Lunin VV, Skarina T, Onopriyenko O, Kohn G, Wins P, De Pauw E, Bettendorff L J Biol Chem. 2011 Sep 30;286(39):34023-35. Epub 2011 Aug 12. PMID:21840996<ref>PMID:21840996</ref>

	~~===The crystal structure~~ of the ~~inorganic triphosphatase NE1496===~~		From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_21840996}}~~		== References ==
			<references/>
	~~==About this Structure==~~		__TOC__
	~~[[3typ]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Nitrosomonas_europaea Nitrosomonas europaea]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3TYP OCA].~~		</StructureSection>

	==~~Reference~~==
	<~~ref group="xtra">PMID:021840996<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Nitrosomonas europaea]]		[[Category: Nitrosomonas europaea]]
	[[Category: Binkowski, T A.]]		[[Category: Binkowski, T A.]]

OCA at 05:04, 1 August 2012

2012-08-01T05:04:03Z

← Older revision		Revision as of 05:04, 1 August 2012
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	[[Image:3typ.~~jpg~~\|left\|200px]]		[[Image:3typ.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_3typ", 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_3typ\| PDB=3typ \| SCENE= }}		{{STRUCTURE_3typ\| PDB=3typ \| SCENE= }}

	===The crystal structure of the inorganic triphosphatase NE1496===		===The crystal structure of the inorganic triphosphatase NE1496===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_21840996}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 21840996 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_21840996}}		{{ABSTRACT_PUBMED_21840996}}

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	[[Category: Joachimiak, A.]]		[[Category: Joachimiak, A.]]
	[[Category: Lunin, V V.]]		[[Category: Lunin, V V.]]
	~~[[Category: MCSG, Midwest Center for Structural Genomics.]]~~
	[[Category: Onopriyenko, O.]]		[[Category: Onopriyenko, O.]]
	[[Category: Savchenko, A.]]		[[Category: Savchenko, A.]]
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	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Inorganic triphosphatase]]		[[Category: Inorganic triphosphatase]]
	~~[[Category: Mcsg]]~~
	~~[[Category: Midwest center for structural genomic]]~~
	~~[[Category: Psi-biology]]~~
	~~[[Category: Structural genomic]]~~

OCA at 09:13, 9 May 2012

2012-05-09T09:13:27Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+[[Image:3typ.jpg|left|200px]]
-The entry 3typ is ON HOLD
+<!--
-Authors: Lunin, V.V., Skarina, T., Onopriyenko, O., Binkowski, T.A., Joachimiak, A., Edwards, A.M., Savchenko, A., Midwest Center for Structural Genomics (MCSG)
+===The crystal structure of the inorganic triphosphatase NE1496===
-Description: The crystal structure of the inorganic triphosphatase NE1496

OCA: Protected "3typ" [edit=sysop:move=sysop]

2011-10-05T06:13:36Z

Protected "3typ" [edit=sysop:move=sysop]

← Older revision	Revision as of 06:13, 5 October 2011
(No difference)

OCA: New page: '''Unreleased structure''' The entry 3typ is ON HOLD Authors: Lunin, V.V., Skarina, T., Onopriyenko, O., Binkowski, T.A., Joachimiak, A., Edwards, A.M., Savchenko, A., Midwest Center fo...

2011-10-05T06:13:34Z

New page: '''Unreleased structure''' The entry 3typ is ON HOLD Authors: Lunin, V.V., Skarina, T., Onopriyenko, O., Binkowski, T.A., Joachimiak, A., Edwards, A.M., Savchenko, A., Midwest Center fo...

New page

'''Unreleased structure'''

The entry 3typ is ON HOLD

Authors: Lunin, V.V., Skarina, T., Onopriyenko, O., Binkowski, T.A., Joachimiak, A., Edwards, A.M., Savchenko, A., Midwest Center for Structural Genomics (MCSG)

Description: The crystal structure of the inorganic triphosphatase NE1496