2ao2

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[[Image:2ao2.gif|left|200px]]
[[Image:2ao2.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2ao2 |SIZE=350|CAPTION= <scene name='initialview01'>2ao2</scene>, resolution 2.070&Aring;
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The line below this paragraph, containing "STRUCTURE_2ao2", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <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>
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or leave the SCENE parameter empty for the default display.
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|GENE= Rv1885c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])
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-->
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK09269 PRK09269]</span>
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{{STRUCTURE_2ao2| PDB=2ao2 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ao2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ao2 OCA], [http://www.ebi.ac.uk/pdbsum/2ao2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ao2 RCSB]</span>
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}}
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'''The 2.07 Angstrom crystal structure of Mycobacterium tuberculosis chorismate mutase reveals unexpected gene duplication and suggests a role in host-pathogen interactions'''
'''The 2.07 Angstrom crystal structure of Mycobacterium tuberculosis chorismate mutase reveals unexpected gene duplication and suggests a role in host-pathogen interactions'''
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[[Category: Qamra, R.]]
[[Category: Qamra, R.]]
[[Category: TBSGC, TB Structural Genomics Consortium.]]
[[Category: TBSGC, TB Structural Genomics Consortium.]]
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[[Category: allostery]]
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[[Category: Allostery]]
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[[Category: chorismate mutase]]
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[[Category: Chorismate mutase]]
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[[Category: gene duplication]]
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[[Category: Gene duplication]]
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[[Category: protein structure initiative]]
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[[Category: Protein structure initiative]]
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[[Category: psi]]
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[[Category: Psi]]
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[[Category: structural genomic]]
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[[Category: Structural genomic]]
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[[Category: tb structural genomics consortium]]
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[[Category: Tb structural genomics consortium]]
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[[Category: tbsgc]]
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[[Category: Tbsgc]]
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[[Category: tryptophan]]
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[[Category: Tryptophan]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:16:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:55:09 2008''
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Revision as of 16:16, 3 May 2008

Image:2ao2.gif

Template:STRUCTURE 2ao2

The 2.07 Angstrom crystal structure of Mycobacterium tuberculosis chorismate mutase reveals unexpected gene duplication and suggests a role in host-pathogen interactions


Overview

Chorismate mutase catalyzes the first committed step toward the biosynthesis of the aromatic amino acids, phenylalanine and tyrosine. While this biosynthetic pathway exists exclusively in the cell cytoplasm, the Mycobacterium tuberculosis enzyme has been shown to be secreted into the extracellular medium. The secretory nature of the enzyme and its existence in M. tuberculosis as a duplicated gene are suggestive of its role in host-pathogen interactions. We report here the crystal structure of homodimeric chorismate mutase (Rv1885c) from M. tuberculosis determined at 2.15 A resolution. The structure suggests possible gene duplication within each subunit of the dimer (residues 35-119 and 130-199) and reveals an interesting proline-rich region on the protein surface (residues 119-130), which might act as a recognition site for protein-protein interactions. The structure also offers an explanation for its regulation by small ligands, such as tryptophan, a feature previously unknown in the prototypical Escherichia coli chorismate mutase. The tryptophan ligand is found to be sandwiched between the two monomers in a dimer contacting residues 66-68. The active site in the "gene-duplicated" monomer is occupied by a sulfate ion and is located in the first half of the polypeptide, unlike in the Saccharomyces cerevisiae (yeast) enzyme, where it is located in the later half. We hypothesize that the M. tuberculosis chorismate mutase might have a role to play in host-pathogen interactions, making it an important target for designing inhibitor molecules against the deadly pathogen.

About this Structure

2AO2 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

The 2.15 A crystal structure of Mycobacterium tuberculosis chorismate mutase reveals an unexpected gene duplication and suggests a role in host-pathogen interactions., Qamra R, Prakash P, Aruna B, Hasnain SE, Mande SC, Biochemistry. 2006 Jun 13;45(23):6997-7005. PMID:16752890 Page seeded by OCA on Sat May 3 19:16:30 2008

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