2f6l: Difference between revisions

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<StructureSection load='2f6l' size='340' side='right'caption='[[2f6l]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='2f6l' size='340' side='right'caption='[[2f6l]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2f6l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F6L FirstGlance]. <br>
<table><tr><td colspan='2'>[[2f6l]] is a 2 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=2F6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F6L FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv1885c ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</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]] 1.7&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [https://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=2f6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f6l OCA], [https://pdbe.org/2f6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f6l RCSB], [https://www.ebi.ac.uk/pdbsum/2f6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f6l 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=2f6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f6l OCA], [https://pdbe.org/2f6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f6l RCSB], [https://www.ebi.ac.uk/pdbsum/2f6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f6l ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/SCMU_MYCTO SCMU_MYCTO]] Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity (By similarity).  
[https://www.uniprot.org/uniprot/SCMU_MYCTU SCMU_MYCTU] Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity.<ref>PMID:15654876</ref> <ref>PMID:15737998</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=2f6l 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=2f6l ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The gene Rv1885c from the genome of Mycobacterium tuberculosis H37Rv encodes a monofunctional and secreted chorismate mutase (*MtCM) with a 33-amino-acid cleavable signal sequence; hence, it belongs to the *AroQ class of chorismate mutases. Consistent with the heterologously expressed *MtCM having periplasmic destination in Escherichia coli and the absence of a discrete periplasmic compartment in M. tuberculosis, we show here that *MtCM secretes into the culture filtrate of M. tuberculosis. *MtCM functions as a homodimer and exhibits a dimeric state of the protein at a concentration as low as 5 nM. *MtCM exhibits simple Michaelis-Menten kinetics with a Km of 0.5 +/- 0.05 mM and a k(cat) of 60 s(-1) per active site (at 37 degrees C and pH 7.5). The crystal structure of *MtCM has been determined at 1.7 A resolution (Protein Data Bank identifier 2F6L). The protein has an all alpha-helical structure, and the active site is formed within a single chain without any contribution from the second chain in the dimer. Analysis of the structure shows a novel fold topology for the protein with a topologically rearranged helix containing Arg134. We provide evidence by site-directed mutagenesis that the residues Arg49, Lys60, Arg72, Thr105, Glu109, and Arg134 constitute the catalytic site; the numbering of the residues includes the signal sequence. Our investigation on the effect of phenylalanine, tyrosine, and tryptophan on *MtCM shows that *MtCM is not regulated by the aromatic amino acids. Consistent with this observation, the X-ray structure of *MtCM does not have an allosteric regulatory site.


Biochemical and structural characterization of the secreted chorismate mutase (Rv1885c) from Mycobacterium tuberculosis H37Rv: an *AroQ enzyme not regulated by the aromatic amino acids.,Kim SK, Reddy SK, Nelson BC, Vasquez GB, Davis A, Howard AJ, Patterson S, Gilliland GL, Ladner JE, Reddy PT J Bacteriol. 2006 Dec;188(24):8638-48. PMID:17146044<ref>PMID:17146044</ref>
==See Also==
 
*[[3D structures of chorismate mutase|3D structures of chorismate mutase]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2f6l" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Chorismate mutase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Myctu]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Gilliland, G L]]
[[Category: Gilliland GL]]
[[Category: Howard, A J]]
[[Category: Howard AJ]]
[[Category: Kim, S K]]
[[Category: Kim SK]]
[[Category: Ladner, J E]]
[[Category: Ladner JE]]
[[Category: Reddy, P T]]
[[Category: Reddy PT]]
[[Category: Dimer]]
[[Category: Helical]]
[[Category: Isomerase]]

Revision as of 09:25, 3 April 2024

X-ray structure of Chorismate Mutase from Mycobacterium TuberculosisX-ray structure of Chorismate Mutase from Mycobacterium Tuberculosis

Structural highlights

2f6l is a 2 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 1.7Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SCMU_MYCTU Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Sasso S, Ramakrishnan C, Gamper M, Hilvert D, Kast P. Characterization of the secreted chorismate mutase from the pathogen Mycobacterium tuberculosis. FEBS J. 2005 Jan;272(2):375-89. PMID:15654876 doi:10.1111/j.1742-4658.2004.04478.x
  2. ↑ 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

2f6l, resolution 1.70Å

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