2ao2
From Proteopedia
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| - | [[Image:2ao2.gif|left|200px]] | + | [[Image:2ao2.gif|left|200px]] |
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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''' | + | {{Structure |
| + | |PDB= 2ao2 |SIZE=350|CAPTION= <scene name='initialview01'>2ao2</scene>, resolution 2.070Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= Rv1885c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis]) | ||
| + | }} | ||
| + | |||
| + | '''The 2.07 Angstrom crystal structure of Mycobacterium tuberculosis chorismate mutase reveals unexpected gene duplication and suggests a role in host-pathogen interactions''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2AO2 is a [ | + | 2AO2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AO2 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16752890 16752890] |
[[Category: Chorismate mutase]] | [[Category: Chorismate mutase]] | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
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[[Category: protein structure initiative]] | [[Category: protein structure initiative]] | ||
[[Category: psi]] | [[Category: psi]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
[[Category: tb structural genomics consortium]] | [[Category: tb structural genomics consortium]] | ||
[[Category: tbsgc]] | [[Category: tbsgc]] | ||
[[Category: tryptophan]] | [[Category: tryptophan]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:51:55 2008'' |
Revision as of 13:51, 20 March 2008
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| , resolution 2.070Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | Rv1885c (Mycobacterium tuberculosis) | ||||||
| Activity: | Chorismate mutase, with EC number 5.4.99.5 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 15:51:55 2008
Categories: Chorismate mutase | Mycobacterium tuberculosis | Single protein | Aruna, B. | Hasnain, S E. | Mande, S C. | Prakash, P. | Qamra, R. | TBSGC, TB Structural Genomics Consortium. | SO4 | TRP | Allostery | Gene duplication | Protein structure initiative | Psi | Structural genomic | Tb structural genomics consortium | Tbsgc | Tryptophan
