1o57
From Proteopedia
(New page: 200px<br /><applet load="1o57" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o57, resolution 2.20Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1o57.gif|left|200px]]<br /><applet load="1o57" size=" | + | [[Image:1o57.gif|left|200px]]<br /><applet load="1o57" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1o57, resolution 2.20Å" /> | caption="1o57, resolution 2.20Å" /> | ||
'''CRYSTAL STRUCTURE OF THE PURINE OPERON REPRESSOR OF BACILLUS SUBTILIS'''<br /> | '''CRYSTAL STRUCTURE OF THE PURINE OPERON REPRESSOR OF BACILLUS SUBTILIS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The purine repressor from Bacillus subtilis, PurR, represses transcription | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1O57 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with SO4, EPE, P6G, 2PE, PG4 and 1PE as [http://en.wikipedia.org/wiki/ligands ligands]. This structure | + | 1O57 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=EPE:'>EPE</scene>, <scene name='pdbligand=P6G:'>P6G</scene>, <scene name='pdbligand=2PE:'>2PE</scene>, <scene name='pdbligand=PG4:'>PG4</scene> and <scene name='pdbligand=1PE:'>1PE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1P41. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O57 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Krahn, J.]] | [[Category: Krahn, J.]] | ||
| - | [[Category: Shin, B | + | [[Category: Shin, B S.]] |
| - | [[Category: Sinha, S | + | [[Category: Sinha, S C.]] |
| - | [[Category: Smith, J | + | [[Category: Smith, J L.]] |
| - | [[Category: Tomchick, D | + | [[Category: Tomchick, D R.]] |
[[Category: Zalkin, H.]] | [[Category: Zalkin, H.]] | ||
[[Category: 1PE]] | [[Category: 1PE]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:13:33 2008'' |
Revision as of 12:13, 21 February 2008
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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.
About this Structure
1O57 is a Single protein structure of sequence from Bacillus subtilis with , , , , and as ligands. 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 Thu Feb 21 14:13:33 2008
Categories: Bacillus subtilis | Single protein | Krahn, J. | Shin, B S. | Sinha, S C. | Smith, J L. | Tomchick, D R. | Zalkin, H. | 1PE | 2PE | EPE | P6G | PG4 | SO4 | Dna binding | Domain recombination | Helix-turn-helix domain | Phosphoribosyltranseferases | Purine operon repressor | Transcription regulation
