2b5a
From Proteopedia
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|PDB= 2b5a |SIZE=350|CAPTION= <scene name='initialview01'>2b5a</scene>, resolution 1.543Å | |PDB= 2b5a |SIZE=350|CAPTION= <scene name='initialview01'>2b5a</scene>, resolution 1.543Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene> | + | |LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= bclIC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1394 Bacillus caldolyticus]) | |GENE= bclIC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1394 Bacillus caldolyticus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b5a OCA], [http://www.ebi.ac.uk/pdbsum/2b5a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b5a RCSB]</span> | ||
}} | }} | ||
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[[Category: Xu, S Y.]] | [[Category: Xu, S Y.]] | ||
[[Category: Zhu, Z.]] | [[Category: Zhu, Z.]] | ||
| - | [[Category: ACY]] | ||
[[Category: helix-turn-helix motif]] | [[Category: helix-turn-helix motif]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:01:42 2008'' |
Revision as of 23:01, 30 March 2008
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| , resolution 1.543Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | bclIC (Bacillus caldolyticus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
C.BclI, Control Element of the BclI Restriction-Modification System
Overview
Protection from DNA invasion is afforded by restriction-modification systems in many bacteria. The efficiency of protection depends crucially on the relative expression levels of restriction versus methytransferase genes. This regulation is provided by a controller protein, named C protein. Studies of the Bcll system in E. coli suggest that C.Bcll functions as a negative regulator for M.Bcll expression, implying that it plays a role in defense against foreign DNA during virus infection. C.Bcll binds (Kd = 14.3 nM) to a 2-fold symmetric C box DNA sequence that overlaps with the putative -35 promoter region upstream of the bcllM and bcllC genes. The C.Bcll fold comprises five alpha helices: two helices form a helix-turn-helix motif, and the remaining three helices form the extensive dimer interface. The C.Bcll-DNA model proposed suggests that DNA bending might play an important role in gene regulation, and that Glu27 and Asp31 in C.Bcll might function critically in the regulation.
About this Structure
2B5A is a Protein complex structure of sequences from Bacillus caldolyticus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the restriction-modification system control element C.Bcll and mapping of its binding site., Sawaya MR, Zhu Z, Mersha F, Chan SH, Dabur R, Xu SY, Balendiran GK, Structure. 2005 Dec;13(12):1837-47. PMID:16338412
Page seeded by OCA on Mon Mar 31 02:01:42 2008
