From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1o57.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1o57.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1o57| PDB=1o57 | SCENE= }} | | {{STRUCTURE_1o57| PDB=1o57 | SCENE= }} |
| | | | |
| - | '''CRYSTAL STRUCTURE OF THE PURINE OPERON REPRESSOR OF BACILLUS SUBTILIS'''
| + | ===CRYSTAL STRUCTURE OF THE PURINE OPERON REPRESSOR OF BACILLUS SUBTILIS=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The purine repressor from Bacillus subtilis, PurR, represses transcription from a number of genes with functions in the synthesis, transport, and metabolism of purines. The 2.2-A crystal structure of PurR reveals a two-domain protein organized as a dimer. The larger C-terminal domain belongs to the PRT structural family, in accord with a sequence motif for binding the inducer phosphoribosylpyrophosphate (PRPP). The PRT domain is fused to a smaller N-terminal domain that belongs to the winged-helix family of DNA binding proteins. A positively charged surface on the winged-helix domain likely binds specific DNA sequences in the recognition site. A second positively charged surface surrounds the PRPP site at the opposite end of the PurR dimer. Conserved amino acids in the sequences of PurR homologs in 21 gram-positive bacteria cluster on the proposed recognition surface of the winged-helix domain and around the PRPP binding site at the opposite end of the molecule, supporting a common function of DNA and PRPP binding for all of the proteins. The structure supports a binding mechanism in which extended regions of DNA interact with extensive protein surface. Unlike most PRT proteins, which are phosphoribosyltransferases (PRTases), PurR lacks catalytic activity. This is explained by a tyrosine side chain that blocks the site for a nucleophile cosubstrate in PRTases. Thus, B. subtilis has adapted an enzyme fold to serve as an effector-binding domain and has used it in a novel combination with the DNA-binding winged-helix domain as a repressor of purine genes. | + | The line below this paragraph, {{ABSTRACT_PUBMED_12837783}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12837783 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_12837783}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 34: |
Line 38: |
| | [[Category: Purine operon repressor]] | | [[Category: Purine operon repressor]] |
| | [[Category: Transcription regulation]] | | [[Category: Transcription regulation]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:23:47 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:20:11 2008'' |
Revision as of 10:20, 28 July 2008
Template:STRUCTURE 1o57
CRYSTAL STRUCTURE OF THE PURINE OPERON REPRESSOR OF BACILLUS SUBTILIS
Template:ABSTRACT PUBMED 12837783
About this Structure
1O57 is a Single protein structure of sequence from Bacillus subtilis. This structure supersedes the now removed PDB entry 1p41. Full crystallographic information is available from OCA.
Reference
The purine repressor of Bacillus subtilis: a novel combination of domains adapted for transcription regulation., Sinha SC, Krahn J, Shin BS, Tomchick DR, Zalkin H, Smith JL, J Bacteriol. 2003 Jul;185(14):4087-98. PMID:12837783
Page seeded by OCA on Mon Jul 28 13:20:11 2008
