1bjo
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1bjo.gif|left|200px]] | + | [[Image:1bjo.gif|left|200px]] |
| - | + | ||
| - | '''THE STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM E. COLI IN COMPLEX WITH ALPHA-METHYL-L-GLUTAMATE''' | + | {{Structure |
| + | |PDB= 1bjo |SIZE=350|CAPTION= <scene name='initialview01'>1bjo</scene>, resolution 2.80Å | ||
| + | |SITE= <scene name='pdbsite=PPA:Plp+Binding+Site.+Site+Site_identifier+Ppb+Site_descript+...'>PPA</scene> and <scene name='pdbsite=PPB:Plp+Binding+Site'>PPB</scene> | ||
| + | |LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoserine_transaminase Phosphoserine transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.52 2.6.1.52] | ||
| + | |GENE= SERC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''THE STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM E. COLI IN COMPLEX WITH ALPHA-METHYL-L-GLUTAMATE''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1BJO is a [ | + | 1BJO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BJO OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 A resolution: comparison of the unligated enzyme and a complex with alpha-methyl-l-glutamate., Hester G, Stark W, Moser M, Kallen J, Markovic-Housley Z, Jansonius JN, J Mol Biol. 1999 Feb 26;286(3):829-50. PMID:[http:// | + | Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 A resolution: comparison of the unligated enzyme and a complex with alpha-methyl-l-glutamate., Hester G, Stark W, Moser M, Kallen J, Markovic-Housley Z, Jansonius JN, J Mol Biol. 1999 Feb 26;286(3):829-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10024454 10024454] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Phosphoserine transaminase]] | [[Category: Phosphoserine transaminase]] | ||
| Line 21: | Line 30: | ||
[[Category: l-serine biosynthesis]] | [[Category: l-serine biosynthesis]] | ||
| - | ''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 10:12:02 2008'' |
Revision as of 08:12, 20 March 2008
| |||||||
| , resolution 2.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | |||||||
| Gene: | SERC (Escherichia coli) | ||||||
| Activity: | Phosphoserine transaminase, with EC number 2.6.1.52 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM E. COLI IN COMPLEX WITH ALPHA-METHYL-L-GLUTAMATE
Overview
Phosphoserine aminotransferase (PSAT; EC 2.6.1.52), a member of subgroup IV of the aminotransferases, catalyses the conversion of 3-phosphohydroxypyruvate to l-phosphoserine. The crystal structure of PSAT from Escherichia coli has been solved in space group P212121 using MIRAS phases in combination with density modification and was refined to an R-factor of 17.5% (Rfree=20.1 %) at 2.3 A resolution. In addition, the structure of PSAT in complex with alpha-methyl-l-glutamate (AMG) has been refined to an R-factor of 18.5% (Rfree=25.1%) at 2.8 A resolution. Each subunit (361 residues) of the PSAT homodimer is composed of a large pyridoxal-5'-phosphate binding domain (residues 16-268), consisting of a seven-stranded mainly parallel beta-sheet, two additional beta-strands and seven alpha-helices, and a small C-terminal domain, which incorporates a five-stranded beta-sheet and two alpha-helices. A three-dimensional structural comparison to four other vitamin B6-dependent enzymes reveals that three alpha-helices of the large domain, as well as an N-terminal domain (subgroup II) or subdomain (subgroup I) are absent in PSAT. Its only 15 N-terminal residues form a single beta-strand, which participates in the beta-sheet of the C-terminal domain. The cofactor is bound through an aldimine linkage to Lys198 in the active site. In the PSAT-AMG complex Ser9 and Arg335 bind the AMG alpha-carboxylate group while His41, Arg42 and His328 are involved in binding the AMG side-chain. Arg77 binds the AMG side-chain indirectly through a solvent molecule and is expected to position itself during catalysis between the PLP phosphate group and the substrate side-chain. Comparison of the active sites of PSAT and aspartate aminotransferase suggests a similar catalytic mechanism, except for the transaldimination step, since in PSAT the Schiff base is protonated. Correlation of the PSAT crystal structure to a published profile sequence analysis of all subgroup IV members allows active site modelling of nifs and the proposal of a likely molecular reaction mechanism.
About this Structure
1BJO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 A resolution: comparison of the unligated enzyme and a complex with alpha-methyl-l-glutamate., Hester G, Stark W, Moser M, Kallen J, Markovic-Housley Z, Jansonius JN, J Mol Biol. 1999 Feb 26;286(3):829-50. PMID:10024454
Page seeded by OCA on Thu Mar 20 10:12:02 2008
