2gbb: Difference between revisions
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<StructureSection load='2gbb' size='340' side='right'caption='[[2gbb]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='2gbb' size='340' side='right'caption='[[2gbb]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2gbb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2gbb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pestis_biovar_Microtus_str._91001 Yersinia pestis biovar Microtus str. 91001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GBB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GBB FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2gbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gbb OCA], [https://pdbe.org/2gbb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gbb RCSB], [https://www.ebi.ac.uk/pdbsum/2gbb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gbb ProSAT]</span></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=2gbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gbb OCA], [https://pdbe.org/2gbb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gbb RCSB], [https://www.ebi.ac.uk/pdbsum/2gbb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gbb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/SCMU_YERPE SCMU_YERPE] Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity.<ref>PMID:18727669</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gb/2gbb_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gb/2gbb_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Yersinia pestis biovar | [[Category: Yersinia pestis biovar Microtus str. 91001]] | ||
[[Category: Kim | [[Category: Kim S-K]] | ||
[[Category: Ladner | [[Category: Ladner JE]] | ||
[[Category: Nelson | [[Category: Nelson BC]] | ||
[[Category: Reddy | [[Category: Reddy PT]] | ||
[[Category: Robinson | [[Category: Robinson H]] | ||
Latest revision as of 11:03, 30 October 2024
Crystal structure of secreted chorismate mutase from Yersinia pestisCrystal structure of secreted chorismate mutase from Yersinia pestis
Structural highlights
FunctionSCMU_YERPE Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe Rv0948c gene from Mycobacterium tuberculosis H(37)R(v) encodes a 90 amino acid protein as the natural gene product with chorismate mutase (CM) activity. The protein, 90-MtCM, exhibits Michaelis-Menten kinetics with a k(cat) of 5.5+/-0.2s(-1) and a K(m) of 1500+/-100microm at 37 degrees C and pH7.5. The 2.0A X-ray structure shows that 90-MtCM is an all alpha-helical homodimer (Protein Data Bank ID: 2QBV) with the topology of Escherichia coli CM (EcCM), and that both protomers contribute to each catalytic site. Superimposition onto the structure of EcCM and the sequence alignment shows that the C-terminus helix3 is shortened. The absence of two residues in the active site of 90-MtCM corresponding to Ser84 and Gln88 of EcCM appears to be one reason for the low k(cat). Hence, 90-MtCM belongs to a subfamily of alpha-helical AroQ CMs termed AroQ(delta.) The CM gene (y2828) from Yersinia pestis encodes a 186 amino acid protein with an N-terminal signal peptide that directs the protein to the periplasm. The mature protein, *YpCM, exhibits Michaelis-Menten kinetics with a k(cat) of 70+/-5s(-1) and K(m) of 500+/-50microm at 37 degrees C and pH7.5. The 2.1A X-ray structure shows that *YpCM is an all alpha-helical protein, and functions as a homodimer, and that each protomer has an independent catalytic unit (Protein Data Bank ID: 2GBB). *YpCM belongs to the AroQ(gamma) class of CMs, and is similar to the secreted CM (Rv1885c, *MtCM) from M.tuberculosis. A comparative biochemical and structural analysis of the intracellular chorismate mutase (Rv0948c) from Mycobacterium tuberculosis H(37)R(v) and the secreted chorismate mutase (y2828) from Yersinia pestis.,Kim SK, Reddy SK, Nelson BC, Robinson H, Reddy PT, Ladner JE FEBS J. 2008 Oct;275(19):4824-35. Epub 2008 Aug 22. PMID:18727669[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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