2qbv

From Proteopedia

(Difference between revisions)

Current revision

Crystal Structure of Intracellular Chorismate Mutase from Mycobacterium Tuberculosis

Structural highlights

2qbv is a 1 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CHMU_MYCTU Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.^[1] ^[2] ^[3]

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 PubMed

The 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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Prakash P, Aruna B, Sardesai AA, Hasnain SE. Purified recombinant hypothetical protein coded by open reading frame Rv1885c of Mycobacterium tuberculosis exhibits a monofunctional AroQ class of periplasmic chorismate mutase activity. J Biol Chem. 2005 May 20;280(20):19641-8. Epub 2005 Feb 28. PMID:15737998 doi:10.1074/jbc.M413026200
↑ Kim SK, Reddy SK, Nelson BC, Robinson H, Reddy PT, Ladner JE. 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. FEBS J. 2008 Oct;275(19):4824-35. Epub 2008 Aug 22. PMID:18727669 doi:10.1111/j.1742-4658.2008.06621.x
↑ Sasso S, Okvist M, Roderer K, Gamper M, Codoni G, Krengel U, Kast P. Structure and function of a complex between chorismate mutase and DAHP synthase: efficiency boost for the junior partner. EMBO J. 2009 Jul 22;28(14):2128-42. Epub 2009 Jun 25. PMID:19556970 doi:10.1038/emboj.2009.165
↑ Kim SK, Reddy SK, Nelson BC, Robinson H, Reddy PT, Ladner JE. 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. FEBS J. 2008 Oct;275(19):4824-35. Epub 2008 Aug 22. PMID:18727669 doi:10.1111/j.1742-4658.2008.06621.x

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2qbv"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Intracellular Chorismate Mutase from Mycobacterium Tuberculosis==
-<StructureSection load='2qbv' size='340' side='right' caption='[[2qbv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='2qbv' size='340' side='right'caption='[[2qbv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2qbv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_h37rv Mycobacterium tuberculosis h37rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QBV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QBV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2qbv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QBV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QBV FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv0948c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 Mycobacterium tuberculosis H37Rv])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] </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=2qbv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qbv OCA], [https://pdbe.org/2qbv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qbv RCSB], [https://www.ebi.ac.uk/pdbsum/2qbv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qbv ProSAT]</span></td></tr>
-<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=2qbv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qbv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2qbv RCSB], [http://www.ebi.ac.uk/pdbsum/2qbv PDBsum]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/CHMU_MYCTU CHMU_MYCTU] Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.<ref>PMID:15737998</ref> <ref>PMID:18727669</ref> <ref>PMID:19556970</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qb/2qbv_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qb/2qbv_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qbv ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 25: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2qbv" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[3D structures of chorismate mutase|3D structures of chorismate mutase]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Chorismate mutase]]
+[[Category: Large Structures]]
-[[Category: Mycobacterium tuberculosis h37rv]]
+[[Category: Mycobacterium tuberculosis H37Rv]]
-[[Category: Kim, S K]]
+[[Category: Kim SK]]
-[[Category: Ladner, J E]]
+[[Category: Ladner JE]]
-[[Category: Nelson, B C]]
+[[Category: Nelson BC]]
-[[Category: Reddy, P T]]
+[[Category: Reddy PT]]
-[[Category: Reddy, S K]]
+[[Category: Reddy S-K]]
-[[Category: Dimeric]]
-[[Category: Helical]]
-[[Category: Intracellular]]
-[[Category: Isomerase]]
-[[Category: Tuberculosis]]

2qbv

From Proteopedia

Current revision

Crystal Structure of Intracellular Chorismate Mutase from Mycobacterium Tuberculosis

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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