3tec - Revision history

OCA at 10:08, 1 March 2024

2024-03-01T10:08:16Z

← Older revision		Revision as of 10:08, 1 March 2024
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	==CALCIUM BINDING TO THERMITASE. CRYSTALLOGRAPHIC STUDIES OF THERMITASE AT 0, 5 AND 100 MM CALCIUM==		==CALCIUM BINDING TO THERMITASE. CRYSTALLOGRAPHIC STUDIES OF THERMITASE AT 0, 5 AND 100 MM CALCIUM==
	<StructureSection load='3tec' size='340' side='right' caption='[[3tec]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3tec' size='340' side='right'caption='[[3tec]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3tec]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/ ] and [~~http~~://en.wikipedia.org/wiki/~~Atcc_43649 Atcc 43649~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TEC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3TEC FirstGlance]. <br>		<table><tr><td colspan='2'>[[3tec]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Poecilobdella_manillensis Poecilobdella manillensis] and [https://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TEC FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=CA:CALCIUM+ION'>CA</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]] 2Å</td></tr>
	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[http://en.wikipedia.org/wiki/Thermitase Thermitase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.66 3.4.21.66]~~ </~~span~~></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=3tec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tec OCA], [~~http~~://pdbe.org/3tec PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3tec RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3tec PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3tec 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=3tec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tec OCA], [https://pdbe.org/3tec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tec RCSB], [https://www.ebi.ac.uk/pdbsum/3tec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tec ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/~~ICIC_HIRME ICIC_HIRME~~]~~] Inhibits both elastase and cathepsin G.~~		[https://www.uniprot.org/uniprot/THET_THEVU THET_THEVU]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		Line 20:
	</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=3tec 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=3tec ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	The three-dimensional crystal structure of thermitase complexed with eglin-c in the presence of 100 mM calcium has been determined and refined at 2.0-A resolution to a R-factor of 16.8%. This crystal structure is compared with previously determined structures of thermitase at 0 and 5 mM calcium concentration. In the presence of 100 mM calcium all three calcium binding sites in thermitase are fully occupied. At 100 mM CaCl2 the "weak" calcium binding is occupied by a calcium ion, which is chelated by three protein ligands and four water molecules in a pentagonal bipyramid geometry. Thermitase has, apparently, a monovalent and divalent cation binding position at 2.5-A distance from each other at this site. At low calcium concentrations the monovalent-ion position is occupied by a sodium or potassium ion. The "medium strength" binding site shows in the presence of 100 mM CaCl2 a square antiprism arrangement with eight ligands, of which seven are donated by the protein. At low calcium concentrations we observe a distorted pentagonal bipyramid coordination at this site. The largest difference between these two conformations is observed for ligand Asp-60, which has two conformations with 0.8-A difference in C alpha positions. The "strong" calcium binding site has a pentagonal bipyramid coordination and is fully occupied in all three structures. Structural changes on binding calcium to the weak and "medium strength" calcium binding sites of thermitase are limited to the direct surroundings of these sites. Thermitase resembles in this respect subtilisin BPN' and does not exhibit long-range shifts as have been reported for proteinase K.

	~~Calcium binding to thermitase. Crystallographic studies of thermitase at 0, 5, and 100 mM calcium.,Gros P, Kalk KH, Hol WG J Biol Chem. 1991 Feb 15;266(5):2953-61. PMID:1993669<ref>PMID:1993669</ref>~~

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 3tec" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Eglin\|Eglin]]		*[[Eglin\|Eglin]]
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Atcc 43649~~]]		[[Category: Large Structures]]
	[[Category: ~~Thermitase~~]]		[[Category: Poecilobdella manillensis]]
	[[Category: Gros, P]]		[[Category: Thermoactinomyces vulgaris]]
	[[Category: Hol~~, W G.J~~]]		[[Category: Gros P]]
	[[Category: Kalk~~, K H~~]]		[[Category: Hol WGJ]]
			[[Category: Kalk KH]]

OCA at 10:50, 13 February 2019

2019-02-13T10:50:39Z

← Older revision		Revision as of 10:50, 13 February 2019
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/te/3tec_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/te/3tec_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 22:03, 5 August 2016

2016-08-05T22:03:21Z

← Older revision		Revision as of 22:03, 5 August 2016
Line 1:		Line 1:

	==CALCIUM BINDING TO THERMITASE. CRYSTALLOGRAPHIC STUDIES OF THERMITASE AT 0, 5 AND 100 MM CALCIUM==		==CALCIUM BINDING TO THERMITASE. CRYSTALLOGRAPHIC STUDIES OF THERMITASE AT 0, 5 AND 100 MM CALCIUM==
	<StructureSection load='3tec' size='340' side='right' caption='[[3tec]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3tec' size='340' side='right' caption='[[3tec]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3tec]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Hirudinaria_manillensis Hirudinaria manillensis~~] and [http://en.wikipedia.org/wiki/~~Thermoactinomyces_vulgaris Thermoactinomyces vulgaris~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TEC FirstGlance]. <br>		<table><tr><td colspan='2'>[[3tec]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Atcc_43649 Atcc 43649]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TEC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thermitase Thermitase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.66 3.4.21.66] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thermitase Thermitase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.66 3.4.21.66] </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=3tec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tec OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tec RCSB], [http://www.ebi.ac.uk/pdbsum/3tec 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=3tec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tec OCA], [http://pdbe.org/3tec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tec RCSB], [http://www.ebi.ac.uk/pdbsum/3tec PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tec ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		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=3tec ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 27:		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 3tec" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Hirudinaria manillensis~~]]		[[Category: Atcc 43649]]
	[[Category: Thermitase]]		[[Category: Thermitase]]
	~~[[Category: Thermoactinomyces vulgaris]]~~
	[[Category: Gros, P]]		[[Category: Gros, P]]
	[[Category: Hol, W G.J]]		[[Category: Hol, W G.J]]
	[[Category: Kalk, K H]]		[[Category: Kalk, K H]]

OCA at 22:17, 25 December 2014

2014-12-25T22:17:27Z

← Older revision		Revision as of 22:17, 25 December 2014
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	<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=3tec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tec OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tec RCSB], [http://www.ebi.ac.uk/pdbsum/3tec 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=3tec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tec OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tec RCSB], [http://www.ebi.ac.uk/pdbsum/3tec PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/ICIC_HIRME ICIC_HIRME]] Inhibits both elastase and cathepsin G.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 16:06, 9 December 2014

2014-12-09T16:06:57Z

← Older revision		Revision as of 16:06, 9 December 2014
Line 1:		Line 1:
	[[Image:~~3tec~~.~~png~~\|~~left~~\|~~200px~~]]		==CALCIUM BINDING TO THERMITASE. CRYSTALLOGRAPHIC STUDIES OF THERMITASE AT 0, 5 AND 100 MM CALCIUM==
			<StructureSection load='3tec' size='340' side='right' caption='[[3tec]], [[Resolution\|resolution]] 2.00Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[3tec]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Hirudinaria_manillensis Hirudinaria manillensis] and [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TEC FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thermitase Thermitase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.66 3.4.21.66] </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=3tec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tec OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tec RCSB], [http://www.ebi.ac.uk/pdbsum/3tec 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/te/3tec_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 ==
			The three-dimensional crystal structure of thermitase complexed with eglin-c in the presence of 100 mM calcium has been determined and refined at 2.0-A resolution to a R-factor of 16.8%. This crystal structure is compared with previously determined structures of thermitase at 0 and 5 mM calcium concentration. In the presence of 100 mM calcium all three calcium binding sites in thermitase are fully occupied. At 100 mM CaCl2 the "weak" calcium binding is occupied by a calcium ion, which is chelated by three protein ligands and four water molecules in a pentagonal bipyramid geometry. Thermitase has, apparently, a monovalent and divalent cation binding position at 2.5-A distance from each other at this site. At low calcium concentrations the monovalent-ion position is occupied by a sodium or potassium ion. The "medium strength" binding site shows in the presence of 100 mM CaCl2 a square antiprism arrangement with eight ligands, of which seven are donated by the protein. At low calcium concentrations we observe a distorted pentagonal bipyramid coordination at this site. The largest difference between these two conformations is observed for ligand Asp-60, which has two conformations with 0.8-A difference in C alpha positions. The "strong" calcium binding site has a pentagonal bipyramid coordination and is fully occupied in all three structures. Structural changes on binding calcium to the weak and "medium strength" calcium binding sites of thermitase are limited to the direct surroundings of these sites. Thermitase resembles in this respect subtilisin BPN' and does not exhibit long-range shifts as have been reported for proteinase K.

	~~{{STRUCTURE_3tec\| PDB=3tec \| SCENE= }}~~		Calcium binding to thermitase. Crystallographic studies of thermitase at 0, 5, and 100 mM calcium.,Gros P, Kalk KH, Hol WG J Biol Chem. 1991 Feb 15;266(5):2953-61. PMID:1993669<ref>PMID:1993669</ref>

	~~===CALCIUM BINDING TO THERMITASE. CRYSTALLOGRAPHIC STUDIES OF THERMITASE AT 0~~, ~~5 AND 100 MM CALCIUM===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_1993669}}~~

	~~==About this Structure==~~
	~~[[3tec]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Hirudinaria_manillensis Hirudinaria manillensis] and [http://en~~.~~wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il~~/~~oca-bin/ocashort?id=3TEC OCA].~~

	==See Also==		==See Also==
	*[[Eglin\|Eglin]]		*[[Eglin\|Eglin]]
			== References ==
	==~~Reference~~==		<references/>
	<~~ref group="xtra">PMID:001993669<~~/~~ref~~><~~references group="xtra"~~/>		__TOC__
			</StructureSection>
	[[Category: Hirudinaria manillensis]]		[[Category: Hirudinaria manillensis]]
	[[Category: Thermitase]]		[[Category: Thermitase]]
	[[Category: Thermoactinomyces vulgaris]]		[[Category: Thermoactinomyces vulgaris]]
	[[Category: Gros, P.]]		[[Category: Gros, P]]
	[[Category: Hol, W G.J.]]		[[Category: Hol, W G.J]]
	[[Category: Kalk, K H.]]		[[Category: Kalk, K H]]

OCA at 22:18, 20 October 2012

2012-10-20T22:18:18Z

← Older revision		Revision as of 22:18, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
	[[3tec]] is a 2 chain structure ~~of [[Eglin]]~~ with sequence from [http://en.wikipedia.org/wiki/Hirudinaria_manillensis Hirudinaria manillensis] and [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TEC OCA].		[[3tec]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Hirudinaria_manillensis Hirudinaria manillensis] and [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TEC OCA].

	==See Also==		==See Also==

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

2012-07-27T15:52:24Z

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

← Older revision	Revision as of 15:52, 27 July 2012
(No difference)

OCA at 15:52, 27 July 2012

2012-07-27T15:52:21Z

← Older revision		Revision as of 15:52, 27 July 2012
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	~~{{Seed}}~~
	[[Image:3tec.png\|left\|200px]]		[[Image:3tec.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_3tec", 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_3tec\| PDB=3tec \| SCENE= }}		{{STRUCTURE_3tec\| PDB=3tec \| SCENE= }}

	===CALCIUM BINDING TO THERMITASE. CRYSTALLOGRAPHIC STUDIES OF THERMITASE AT 0, 5 AND 100 MM CALCIUM===		===CALCIUM BINDING TO THERMITASE. CRYSTALLOGRAPHIC STUDIES OF THERMITASE AT 0, 5 AND 100 MM CALCIUM===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_1993669}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 1993669 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_1993669}}		{{ABSTRACT_PUBMED_1993669}}

	==About this Structure==		==About this Structure==
	~~3TEC~~ is a 2 ~~chains~~ structure of ~~sequences~~ from [http://en.wikipedia.org/wiki/Hirudinaria_manillensis Hirudinaria manillensis] and [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TEC OCA].		[[3tec]] is a 2 chain structure of [[Eglin]] with sequence from [http://en.wikipedia.org/wiki/Hirudinaria_manillensis Hirudinaria manillensis] and [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TEC OCA].

			==See Also==
			*[[Eglin\|Eglin]]

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~1993669~~</ref><references group="xtra"/>		<ref group="xtra">PMID:001993669</ref><references group="xtra"/>
	[[Category: Hirudinaria manillensis]]		[[Category: Hirudinaria manillensis]]
	[[Category: Thermitase]]		[[Category: Thermitase]]
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	[[Category: Hol, W G.J.]]		[[Category: Hol, W G.J.]]
	[[Category: Kalk, K H.]]		[[Category: Kalk, K H.]]

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	==About this Structure==		==About this Structure==
	3TEC is a ~~[[Protein complex]]~~ structure of sequences from [http://en.wikipedia.org/wiki/Hirudinaria_manillensis Hirudinaria manillensis] and [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TEC OCA].		3TEC is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Hirudinaria_manillensis Hirudinaria manillensis] and [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TEC OCA].

	==Reference==		==Reference==
	~~Calcium binding to thermitase. Crystallographic studies of thermitase at 0, 5, and 100 mM calcium., Gros P, Kalk KH, Hol WG, J Biol Chem. 1991 Feb 15;266(5):2953-61.~~ PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/1993669 1993669]~~		<ref group="xtra">PMID:1993669</ref><references group="xtra"/>
	[[Category: Hirudinaria manillensis]]		[[Category: Hirudinaria manillensis]]
	~~[[Category: Protein complex]]~~
	[[Category: Thermitase]]		[[Category: Thermitase]]
	[[Category: Thermoactinomyces vulgaris]]		[[Category: Thermoactinomyces vulgaris]]
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	[[Category: Kalk, K H.]]		[[Category: Kalk, K H.]]

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	[[Image:3tec.~~jpg~~\|left\|200px]]		{{Seed}}
			[[Image:3tec.png\|left\|200px]]

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	{{STRUCTURE_3tec\| PDB=3tec \| SCENE= }}		{{STRUCTURE_3tec\| PDB=3tec \| SCENE= }}

	~~'''~~CALCIUM BINDING TO THERMITASE. CRYSTALLOGRAPHIC STUDIES OF THERMITASE AT 0, 5 AND 100 MM CALCIUM~~'''~~		===CALCIUM BINDING TO THERMITASE. CRYSTALLOGRAPHIC STUDIES OF THERMITASE AT 0, 5 AND 100 MM CALCIUM===


	~~==Overview==~~		<!--
	The ~~three-dimensional crystal structure of thermitase complexed with eglin-c in~~ the ~~presence of 100 mM calcium has been determined and refined at 2.0-A resolution~~ to ~~a R-factor of 16.8%. This crystal structure is compared with previously determined structures of thermitase~~ at ~~0 and 5 mM calcium concentration~~. ~~In the presence of 100 mM calcium all three calcium binding sites in thermitase are fully occupied~~. ~~At 100 mM CaCl2 the "weak" calcium binding is occupied by a calcium ion~~, which is chelated by three protein ligands and four water molecules in a pentagonal bipyramid geometry. Thermitase has, apparently, a monovalent and divalent cation binding position at 2.5-A distance from each other at this site. At low calcium concentrations the monovalent-ion position is ~~occupied by a sodium or potassium ion. The "medium strength" binding site shows in the presence of 100 mM CaCl2 a square antiprism arrangement with eight ligands, of which seven are donated by~~ the ~~protein~~. At low calcium concentrations we observe a distorted pentagonal bipyramid coordination at this site. The largest difference between these two conformations is observed for ligand Asp-60, which has two conformations with 0.8-A difference in C alpha positions. The "strong" calcium binding site has a pentagonal bipyramid coordination and is fully occupied in all three structures. Structural changes on binding calcium to the weak and "medium strength" calcium binding sites of thermitase are limited to the direct surroundings of these sites. Thermitase resembles in this respect subtilisin BPN' and does not exhibit long-~~range shifts as have been reported for proteinase K.~~		The line below this paragraph, {{ABSTRACT_PUBMED_1993669}}, adds the Publication Abstract to the page
			(as it appears on PubMed at http://www.pubmed.gov), where 1993669 is the PubMed ID number.
			-->
			{{ABSTRACT_PUBMED_1993669}}

	==About this Structure==		==About this Structure==
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	[[Category: Hol, W G.J.]]		[[Category: Hol, W G.J.]]
	[[Category: Kalk, K H.]]		[[Category: Kalk, K H.]]
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