4ov4: Difference between revisions
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==Isopropylmalate synthase binding with ketoisovalerate== | ==Isopropylmalate synthase binding with ketoisovalerate== | ||
<StructureSection load='4ov4' size='340' side='right' caption='[[4ov4]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='4ov4' size='340' side='right'caption='[[4ov4]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ov4]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ov4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leptospira_biflexa_serovar_Patoc_strain_'Patoc_1_(Paris)' Leptospira biflexa serovar Patoc strain 'Patoc 1 (Paris)']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OV4 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KIV:3-METHYL-2-OXOBUTANOIC+ACID'>KIV</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KIV:3-METHYL-2-OXOBUTANOIC+ACID'>KIV</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4ov4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ov4 OCA], [https://pdbe.org/4ov4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ov4 RCSB], [https://www.ebi.ac.uk/pdbsum/4ov4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ov4 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/B0SN40_LEPBP B0SN40_LEPBP] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[2-isopropylmalate synthase|2-isopropylmalate synthase]] | *[[2-isopropylmalate synthase 3D structures|2-isopropylmalate synthase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Wang C]] | |||
[[Category: Wang | [[Category: Wu J]] | ||
[[Category: Wu | [[Category: Zhang P]] | ||
[[Category: Zhang | [[Category: Zhang Z]] | ||
[[Category: Zhang | |||
Revision as of 10:47, 25 January 2023
Isopropylmalate synthase binding with ketoisovalerateIsopropylmalate synthase binding with ketoisovalerate
Structural highlights
FunctionPublication Abstract from PubMedThe committed step of leucine biosynthesis, converting acetyl-CoA and alpha-ketoisovalerate into alpha-isopropylmalate, is catalyzed by alpha-isopropylmalate synthase (IPMS), an allosteric enzyme subjected to feedback inhibition by the end product L-leucine. We characterized the short form IPMS from Leptospira biflexa (LbIPMS2), which exhibits a catalytic activity comparable with that of the long form IPMS (LbIPMS1) and has a similar N-terminal domain followed by subdomain I and subdomain II but lacks the whole C-terminal regulatory domain. We found that partial deletion of the regulatory domain of LbIPMS1 resulted in a loss of about 50% of the catalytic activity; however, when the regulatory domain was deleted up to Arg-385, producing a protein that is almost equivalent to the intact LbIPMS2, about 90% of the activity was maintained. Moreover, in LbIPMS2 or LbIPMS1, further deletion of several residues from the C terminus of subdomain II significantly impaired or completely abolished the catalytic activity, respectively. These results define a complete and independently functional catalytic module of IPMS consisting of both the N-terminal domain and the two subdomains. Structural comparison of LbIPMS2 and the Mycobacterium tuberculosis IPMS revealed two different conformations of subdomain II that likely represent two substrate-binding states related to cooperative catalysis. The biochemical and structural analyses together with the previously published hydrogen-deuterium exchange data led us to propose a conformation transition mechanism for feedback inhibition mediated by subdomains I and II that might associated with alteration of the binding affinity toward acetyl-CoA. Subdomain II of alpha-isopropylmalate synthase is essential for activity: inferring a mechanism of feedback inhibition.,Zhang Z, Wu J, Lin W, Wang J, Yan H, Zhao W, Ma J, Ding J, Zhang P, Zhao GP J Biol Chem. 2014 Oct 3;289(40):27966-78. doi: 10.1074/jbc.M114.559716. Epub 2014, Aug 15. PMID:25128527[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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