5yei

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==Mechanistic insight into the regulation of Pseudomonas aeruginosa aspartate kinase==
==Mechanistic insight into the regulation of Pseudomonas aeruginosa aspartate kinase==
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<StructureSection load='5yei' size='340' side='right' caption='[[5yei]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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<StructureSection load='5yei' size='340' side='right'caption='[[5yei]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5yei]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YEI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YEI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5yei]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YEI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5YEI FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LYS:LYSINE'>LYS</scene>, <scene name='pdbligand=THR:THREONINE'>THR</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LYS:LYSINE'>LYS</scene>, <scene name='pdbligand=THR:THREONINE'>THR</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lysC, PA0904 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_kinase Aspartate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.4 2.7.2.4] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_kinase Aspartate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.4 2.7.2.4] </span></td></tr>
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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=5yei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yei OCA], [http://pdbe.org/5yei PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yei RCSB], [http://www.ebi.ac.uk/pdbsum/5yei PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yei ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5yei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yei OCA], [http://pdbe.org/5yei PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yei RCSB], [http://www.ebi.ac.uk/pdbsum/5yei PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yei ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In plants and microorganisms, aspartate kinase (AK) catalyzes an initial commitment step of the aspartate family amino acid biosynthesis. Owing to various structural organizations, AKs from different species show tremendous diversity and complex allosteric controls. We report the crystal structure of AK from Pseudomonas aeruginosa (PaAK), a typical alpha2beta2 hetero-tetrameric enzyme, in complex with inhibitory effectors. Distinctive features of PaAK are revealed by structural and biochemical analyses. Essentially, the open conformation of Lys-/Thr-bound PaAK structure clarifies the inhibitory mechanism of alpha2beta2-type AK. Moreover, the various inhibitory effectors of PaAK have been identified and a general amino acid effector motif of AK family is described.
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Mechanistic insights into the allosteric regulation of Pseudomonas aeruginosa aspartate kinase.,Li CC, Yang MJ, Liu L, Li T, Peng CT, He LH, Song YJ, Zhu YB, Shen YL, Yang J, Zhao NL, Zhao C, Zhou QX, Li H, Kang M, Tong AP, Tang H, Bao R Biochem J. 2018 Mar 20;475(6):1107-1119. doi: 10.1042/BCJ20170829. PMID:29382741<ref>PMID:29382741</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5yei" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Aspartate kinase]]
[[Category: Aspartate kinase]]
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[[Category: Large Structures]]
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[[Category: Pseae]]
[[Category: Bao, R]]
[[Category: Bao, R]]
[[Category: He, L]]
[[Category: He, L]]

Revision as of 09:17, 21 October 2020

Mechanistic insight into the regulation of Pseudomonas aeruginosa aspartate kinase

PDB ID 5yei

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