1o57: Difference between revisions
New page: left|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]] | ||
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