2q9h: Difference between revisions
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'''Crystal structure of the C73S mutant of diaminopimelate epimerase''' | {{Structure | ||
|PDB= 2q9h |SIZE=350|CAPTION= <scene name='initialview01'>2q9h</scene>, resolution 2.3Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Diaminopimelate_epimerase Diaminopimelate epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.7 5.1.1.7] | |||
|GENE= dapF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae]) | |||
}} | |||
'''Crystal structure of the C73S mutant of diaminopimelate epimerase''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2Q9H is a [ | 2Q9H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q9H OCA]. | ||
==Reference== | ==Reference== | ||
Dynamics of catalysis revealed from the crystal structures of mutants of diaminopimelate epimerase., Pillai B, Cherney M, Diaper CM, Sutherland A, Blanchard JS, Vederas JC, James MN, Biochem Biophys Res Commun. 2007 Nov 23;363(3):547-53. Epub 2007 Sep 17. PMID:[http:// | Dynamics of catalysis revealed from the crystal structures of mutants of diaminopimelate epimerase., Pillai B, Cherney M, Diaper CM, Sutherland A, Blanchard JS, Vederas JC, James MN, Biochem Biophys Res Commun. 2007 Nov 23;363(3):547-53. Epub 2007 Sep 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17889830 17889830] | ||
[[Category: Diaminopimelate epimerase]] | [[Category: Diaminopimelate epimerase]] | ||
[[Category: Haemophilus influenzae]] | [[Category: Haemophilus influenzae]] | ||
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[[Category: c73s mutant]] | [[Category: c73s mutant]] | ||
[[Category: isomerase]] | [[Category: isomerase]] | ||
[[Category: two structurally equivalent | [[Category: two structurally equivalent domain]] | ||
''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 18:23:24 2008'' |
Revision as of 19:23, 20 March 2008
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, resolution 2.3Å | |||||||
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Ligands: | and | ||||||
Gene: | dapF (Haemophilus influenzae) | ||||||
Activity: | Diaminopimelate epimerase, with EC number 5.1.1.7 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of the C73S mutant of diaminopimelate epimerase
OverviewOverview
Diaminopimelate (DAP) epimerase catalyzes the stereoinversion of ll-DAP to meso-DAP, a precursor of l-lysine and an essential component of the bacterial peptidoglycan. This function is vital to bacteria and the enzyme therefore represents an attractive target for the design of novel anti-bacterials. DAP epimerase belongs to the group of PLP-independent amino acid racemases that function through a rather unusual mechanism involving two cysteines acting in concert as a base (thiolate) and an acid (thiol). We have solved the crystal structures of the apo-forms of DAP epimerase mutants (C73S and C217S) from Haemophilus influenzae at 2.3A and 2.2A resolution, respectively. These structures provide a snapshot of the enzyme in the first step of the catalytic cycle. Comparisons with the structures of the inhibitor-bound form reveal that the enzyme adopts an 'open conformation' in the absence of substrates or inhibitors with the two active site cysteines existing as a thiol-thiolate pair. Substrate binding to the C-terminal domain triggers the closure of the N-terminal domain coupled with tight encapsulation of the ligand, stabilization of the conformation of an active site loop containing Cys73 and expulsion of water molecules with concomitant desolvation of the thiolate base. This structural rearrangement is critical for catalysis.
About this StructureAbout this Structure
2Q9H is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.
ReferenceReference
Dynamics of catalysis revealed from the crystal structures of mutants of diaminopimelate epimerase., Pillai B, Cherney M, Diaper CM, Sutherland A, Blanchard JS, Vederas JC, James MN, Biochem Biophys Res Commun. 2007 Nov 23;363(3):547-53. Epub 2007 Sep 17. PMID:17889830
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