1jt0: Difference between revisions

Revision as of 20:45, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1jt0.png

Template:STRUCTURE 1jt0

Crystal structure of a cooperative QacR-DNA complexCrystal structure of a cooperative QacR-DNA complex

Template:ABSTRACT PUBMED 11867549

About this StructureAbout this Structure

1JT0 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for cooperative DNA binding by two dimers of the multidrug-binding protein QacR., Schumacher MA, Miller MC, Grkovic S, Brown MH, Skurray RA, Brennan RG, EMBO J. 2002 Mar 1;21(5):1210-8. PMID:11867549

Page seeded by OCA on Tue Jul 1 20:45:36 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1jt0.gif|left|200px]]
+{{Seed}}
+[[Image:1jt0.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1jt0|  PDB=1jt0  |  SCENE=  }}
-'''Crystal structure of a cooperative QacR-DNA complex'''
+===Crystal structure of a cooperative QacR-DNA complex===
-==Overview==
+<!--
-The Staphylococcus aureus multidrug-binding protein QacR represses transcription of the qacA multidrug transporter gene and is induced by multiple structurally dissimilar drugs. QacR is a member of the TetR/CamR family of transcriptional regulators, which share highly homologous N-terminal DNA-binding domains connected to seemingly non-homologous ligand-binding domains. Unlike other TetR members, which bind approximately 15 bp operators, QacR recognizes an unusually long 28 bp operator, IR1, which it appears to bind cooperatively. To elucidate the DNA-binding mechanism of QacR, we determined the 2.90 A resolution crystal structure of a QacR-IR1 complex. Strikingly, our data reveal that the DNA recognition mode of QacR is distinct from TetR and involves the binding of a pair of QacR dimers. In this unique binding mode, recognition at each IR1 half-site is mediated by a complement of DNA contacts made by two helix-turn-helix motifs. The inferred cooperativity does not arise from cross-dimer protein-protein contacts, but from the global undertwisting and major groove widening elicited by the binding of two QacR dimers.
+The line below this paragraph, {{ABSTRACT_PUBMED_11867549}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11867549 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11867549}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Dimer of dimer]]
 [[Category: Multidrug binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:52:21 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 20:45:36 2008''