7o1j - Revision history

OCA at 12:43, 1 February 2024

OCA — Thu, 01 Feb 2024 12:43:07 GMT

←Older revision		Revision as of 12:43, 1 February 2024
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-	====	+	==Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme beta-C92A mutant==
-	<StructureSection load='7o1j' size='340' side='right'caption='[[7o1j]]' scene=''>	+	<StructureSection load='7o1j' size='340' side='right'caption='[[7o1j]], [[Resolution\|resolution]] 2.36Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7o1j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O1J FirstGlance]. <br>
-	</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=7o1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o1j OCA], [https://pdbe.org/7o1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o1j RCSB], [https://www.ebi.ac.uk/pdbsum/7o1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o1j ProSAT]</span></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]] 2.36Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=7o1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o1j OCA], [https://pdbe.org/7o1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o1j RCSB], [https://www.ebi.ac.uk/pdbsum/7o1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o1j ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/Y0859_MYCTU Y0859_MYCTU]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The Mycobacterium tuberculosis trifunctional enzyme (MtTFE) is an alpha2beta2 tetrameric enzyme. The alpha-chain harbors the 2E-enoyl-CoA hydratase (ECH) and 3S-hydroxyacyl-CoA dehydrogenase (HAD) activities and the beta-chain provides the 3-ketoacyl-CoA thiolase (KAT) activity. Enzyme kinetic data reported here show that medium and long chain enoyl-CoA molecules are preferred substrates for MtTFE. Modelling studies indicate how the linear medium and long acyl chains of these substrates can bind to each of the active sites. In addition, crystallographic binding studies have identified three new CoA binding sites which are different from the previously known CoA binding sites of the three TFE active sites. Structure comparisons provide new insights into the properties of ECH, HAD and KAT active sites of MtTFE. The interactions of the adenine moiety of CoA with loop-2 of the ECH active site cause a conformational change of this loop by which a competent ECH active site is formed. The NAD(+) binding domain (domain C) of the HAD part of MtTFE has only a few interactions with the rest of the complex and adopts a range of open conformations, whereas the A-domain of the ECH part is rigidly fixed with respect to the HAD part. Two loops, the CB1-CA1 region and the catalytic CB4-CB5 loop, near the thiolase active site and the thiolase dimer interface, have high B-factors. Structure comparisons suggest that a competent and stable thiolase dimer is formed only when complexed with the alpha-chains, highlighting the importance of the assembly for the proper functioning of the complex.
		+
		+	Substrate specificity and conformational flexibility properties of the Mycobacterium tuberculosis beta-oxidation trifunctional enzyme.,Dalwani S, Lampela O, Leprovost P, Schmitz W, Juffer AH, Wierenga RK, Venkatesan R J Struct Biol. 2021 Aug 8;213(3):107776. doi: 10.1016/j.jsb.2021.107776. PMID:34371166<ref>PMID:34371166</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7o1j" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Z-disk~~]]	+	[[Category: Mycobacterium tuberculosis H37Rv]]
		+	[[Category: Dalwani S]]
		+	[[Category: Venkatesan R]]
		+	[[Category: Wierenga RK]]

OCA at 06:20, 25 August 2021

OCA — Wed, 25 Aug 2021 06:20:33 GMT

←Older revision		Revision as of 06:20, 25 August 2021
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-	'''Unreleased structure'''

-	~~The entry~~ 7o1j ~~is ON HOLD until Paper Publication~~	+	====
-		+	<StructureSection load='7o1j' size='340' side='right'caption='[[7o1j]]' scene=''>
-	~~Authors~~: ~~Dalwani, S~~.~~, Wierenga, R~~.K.~~, Venkatesan, R~~.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
-	~~Description~~: ~~Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme beta-C92A mutant~~	+	</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=7o1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o1j OCA], [https://pdbe.org/7o1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o1j RCSB], [https://www.ebi.ac.uk/pdbsum/7o1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o1j ProSAT]</span></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	</table>
-	[[~~Category~~: ~~Dalwani~~, S]]	+	__TOC__
-	[[Category: ~~Venkatesan, R~~]]	+	</StructureSection>
-	[[Category: ~~Wierenga, R.K~~]]	+	[[Category: Large Structures]]
		+	[[Category: Z-disk]]

OCA at 04:24, 28 April 2021

OCA — Wed, 28 Apr 2021 04:24:29 GMT

←Older revision		Revision as of 04:24, 28 April 2021
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 7o1j is ON HOLD	+	The entry 7o1j is ON HOLD until Paper Publication

	Authors: Dalwani, S., Wierenga, R.K., Venkatesan, R.		Authors: Dalwani, S., Wierenga, R.K., Venkatesan, R.
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	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Dalwani, S]]		[[Category: Dalwani, S]]
-	[[Category: Wierenga, R.K]]
	[[Category: Venkatesan, R]]		[[Category: Venkatesan, R]]
		+	[[Category: Wierenga, R.K]]

OCA: Protected "7o1j" [edit=sysop:move=sysop]

OCA — Wed, 07 Apr 2021 04:52:19 GMT

Protected "7o1j" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:52, 7 April 2021

OCA: New page: '''Unreleased structure''' The entry 7o1j is ON HOLD Authors: Dalwani, S., Wierenga, R.K., Venkatesan, R. Description: Structure of Mycobacterium tuberculosis beta-oxidation trifunctio...

OCA — Wed, 07 Apr 2021 04:52:18 GMT

New page: '''Unreleased structure''' The entry 7o1j is ON HOLD Authors: Dalwani, S., Wierenga, R.K., Venkatesan, R. Description: Structure of Mycobacterium tuberculosis beta-oxidation trifunctio...

New page

'''Unreleased structure'''

The entry 7o1j is ON HOLD

Authors: Dalwani, S., Wierenga, R.K., Venkatesan, R.

Description: Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme beta-C92A mutant
[[Category: Unreleased Structures]]
[[Category: Dalwani, S]]
[[Category: Wierenga, R.K]]
[[Category: Venkatesan, R]]