4ov4: Difference between revisions

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 == Structural highlights ==
 <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" id="ligandDat"><scene name='pdbligand=KIV:3-METHYL-2-OXOBUTANOIC+ACID'>KIV</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2&#8491;</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>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/B0SN40_LEPBP B0SN40_LEPBP]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The 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<ref>PMID:25128527</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4ov4" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[2-isopropylmalate synthase 3D structures|2-isopropylmalate synthase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>