2q3d: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 2q3d |SIZE=350|CAPTION= <scene name='initialview01'>2q3d</scene>, resolution 2.20Å | |PDB= 2q3d |SIZE=350|CAPTION= <scene name='initialview01'>2q3d</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=PDA:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL)-AMINO]-PROPIONIC+ACID'>PDA</scene> | |LIGAND= <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PDA:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL)-AMINO]-PROPIONIC+ACID'>PDA</scene> | ||
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cysteine_synthase Cysteine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.47 2.5.1.47] </span> | |||
|GENE= cysK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis]) | |GENE= cysK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2q3b|2Q3B]], [[2q3c|2Q3C]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3d OCA], [http://www.ebi.ac.uk/pdbsum/2q3d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2q3d RCSB]</span> | |||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Schneider, G.]] | [[Category: Schneider, G.]] | ||
[[Category: Schnell, R.]] | [[Category: Schnell, R.]] | ||
[[Category: alpha-aminoacrylate intermediate]] | [[Category: alpha-aminoacrylate intermediate]] | ||
[[Category: cysteine biosynthesis]] | [[Category: cysteine biosynthesis]] | ||
| Line 33: | Line 34: | ||
[[Category: sulphur metabolism]] | [[Category: sulphur metabolism]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:44:05 2008'' | ||
Revision as of 04:44, 31 March 2008
| |||||||
| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | cysK (Mycobacterium tuberculosis) | ||||||
| Activity: | Cysteine synthase, with EC number 2.5.1.47 | ||||||
| Related: | 2Q3B, 2Q3C
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
2.2 A Resolution Crystal Structure of O-Acetylserine Sulfhydrylase (OASS) From MYCOBACTERIUM TUBERCULOSIS in Complex with the Reaction Intermediate ALPHA-AMINOACRYLATE
OverviewOverview
Cysteine biosynthetic genes are up-regulated in the persistent phase of Mycobacterium tuberculosis, and the corresponding enzymes are therefore of interest as potential targets for novel antibacterial agents. cysK1 is one of these genes and has been annotated as coding for an O-acetylserine sulfhydrylase. Recombinant CysK1 is a pyridoxal phosphate (PLP)-dependent enzyme that catalyzes the conversion of O-acetylserine to cysteine. The crystal structure of the enzyme was determined to 1.8A resolution. CysK1 belongs to the family of fold type II PLP enzymes and is similar in structure to other O-acetylserine sulfhydrylases. We were able to trap the alpha-aminoacrylate reaction intermediate and determine its structure by cryocrystallography. Formation of the aminoacrylate complex is accompanied by a domain rotation resulting in active site closure. The aminoacrylate moiety is bound in the active site via the covalent linkage to the PLP cofactor and by hydrogen bonds of its carboxyl group to several enzyme residues. The catalytic lysine residue is positioned such that it can protonate the Calpha-carbon atom of the aminoacrylate only from the si-face, resulting in the formation of L-cysteine. CysK1 is competitively inhibited by a four-residue peptide derived from the C-terminal of serine acetyl transferase. The crystallographic analysis reveals that the peptide binds to the enzyme active site, suggesting that CysK1 forms an bi-enzyme complex with serine acetyl transferase, in a similar manner to other bacterial and plant O-acetylserine sulfhydrylases. The structure of the enzyme-peptide complex provides a framework for the design of strong binding inhibitors.
About this StructureAbout this Structure
2Q3D is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
ReferenceReference
Structural insights into catalysis and inhibition of O-acetylserine sulfhydrylase from Mycobacterium tuberculosis. Crystal structures of the enzyme alpha-aminoacrylate intermediate and an enzyme-inhibitor complex., Schnell R, Oehlmann W, Singh M, Schneider G, J Biol Chem. 2007 Aug 10;282(32):23473-81. Epub 2007 Jun 13. PMID:17567578
Page seeded by OCA on Mon Mar 31 04:44:05 2008