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6j2l

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Current revision (10:36, 27 March 2024) (edit) (undo)
 
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<StructureSection load='6j2l' size='340' side='right'caption='[[6j2l]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
<StructureSection load='6j2l' size='340' side='right'caption='[[6j2l]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6j2l]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J2L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6J2L FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6j2l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J2L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6J2L 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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.17&#8491;</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=6j2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j2l OCA], [http://pdbe.org/6j2l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j2l RCSB], [http://www.ebi.ac.uk/pdbsum/6j2l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j2l ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6j2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j2l OCA], [https://pdbe.org/6j2l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6j2l RCSB], [https://www.ebi.ac.uk/pdbsum/6j2l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6j2l ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/HIS2_SHIFL HIS2_SHIFL]
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Histidine biosynthesis, which is absent in animals, was shown to be highly conserved among gram-negative bacteria, thus making it an attractive target for antibiotic design. There are many fusion forms of enzymes in the histidine biosynthetic pathway and people still have limited knowledge about their domain organizations and catalytic mechanisms, due to the lack of structural information. Here we report the first crystal structure of Shigella flexneri bi-functional enzyme HisIE (SfHisIE) that functions in the 2nd and 3rd steps in the histidine biosynthetic pathway. This structure shows that HisIE exists as dimers with two loops (fusion loop) connecting the individual dimer of HisE and HisI in its N-terminus and C-terminus respectively. Our mutagenesis study shows mutations in this fusion loop are lethal for bacteria indicating the advantage of gene fusion in Histidine biosynthesis. Structural analysis revealed several highly conserved residues in the putative ligand binding grooves of HisE and HisI, showing an evolutionarily conserved catalytic mechanism shared among gram negative-bacteria.
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Structural analysis of Shigella flexneri bi-functional enzyme HisIE in histidine biosynthesis.,Wang Y, Zhang F, Nie Y, Shang G, Zhang H Biochem Biophys Res Commun. 2019 Aug 20;516(2):540-545. doi:, 10.1016/j.bbrc.2019.06.099. Epub 2019 Jun 22. PMID:31235255<ref>PMID:31235255</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 6j2l" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Shang, G]]
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[[Category: Shigella flexneri]]
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[[Category: Wang, Y]]
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[[Category: Shang G]]
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[[Category: Zhang, H]]
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[[Category: Wang Y]]
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[[Category: Bi-functional enzyme]]
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[[Category: Zhang H]]
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[[Category: Hydrolase]]
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Current revision

Crystal structure of Bi-functional enzyme

PDB ID 6j2l

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