From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1sft.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1sft.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1sft| PDB=1sft | SCENE= }} | | {{STRUCTURE_1sft| PDB=1sft | SCENE= }} |
| | | | |
| - | '''ALANINE RACEMASE'''
| + | ===ALANINE RACEMASE=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The molecular structure of alanine racemase from Bacillus stearothermophilus was determined by X-ray crystallography to a resolution of 1.9 A. The alanine racemase monomer is composed of two domains, an eight-stranded alpha/beta barrel at the N-terminus, which includes residues 1-240, and a C-terminal domain essentially composed of beta-strand (residues 241-388). In the structure of the dimer the mouth of the alpha/beta barrel of one monomer faces the second domain of the other monomer. The pyridoxal 5'-phosphate (PLP) cofactor lies in and above the mouth of the alpha/beta barrel and is covalently linked via an aldimine linkage to Lys39, which is at the C-terminus of the first beta-strand of the alpha/beta barrel. This is the first example of a PLP cofactor binding in the active site of a alpha/beta barrel. A number of other residues are involved in maintaining the position of the PLP in the protein. Of these, Arg219 is the most interesting, as it forms a hydrogen bond with the pyridine nitrogen of the cofactor. This is the first known occurrence of such an interaction with PLP and is expected to influence the electron delocalization in the PLP-alanine intermediates. A second arginine residue, Arg136, donates a hydrogen bond to the phenolic oxygen of PLP and may be involved in the binding of substrate as well as stabilization of intermediates. Finally, Tyr265', from the second monomer, is postulated to be 2 proton donor to the carbanion intermediate. | + | The line below this paragraph, {{ABSTRACT_PUBMED_9063881}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9063881 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_9063881}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 29: |
Line 33: |
| | [[Category: Isomerase]] | | [[Category: Isomerase]] |
| | [[Category: Pyridoxal phosphate]] | | [[Category: Pyridoxal phosphate]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:38:53 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:35:40 2008'' |
Revision as of 06:35, 29 July 2008
Template:STRUCTURE 1sft
ALANINE RACEMASE
Template:ABSTRACT PUBMED 9063881
About this Structure
1SFT is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
Reference
Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution., Shaw JP, Petsko GA, Ringe D, Biochemistry. 1997 Feb 11;36(6):1329-42. PMID:9063881
Page seeded by OCA on Tue Jul 29 09:35:40 2008
