3bp8: Difference between revisions

Revision as of 00:18, 29 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:3bp8.jpg

Template:STRUCTURE 3bp8

Crystal structure of Mlc/EIIB complexCrystal structure of Mlc/EIIB complex

Template:ABSTRACT PUBMED 18319344

About this StructureAbout this Structure

3BP8 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Analyses of Mlc-IIBGlc interaction and a plausible molecular mechanism of Mlc inactivation by membrane sequestration., Nam TW, Jung HI, An YJ, Park YH, Lee SH, Seok YJ, Cha SS, Proc Natl Acad Sci U S A. 2008 Mar 11;105(10):3751-6. Epub 2008 Mar 4. PMID:18319344

Page seeded by OCA on Tue Jul 29 00:18:14 2008

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

OCA

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 {{STRUCTURE_3bp8|  PDB=3bp8  |  SCENE=  }}
-'''Crystal structure of Mlc/EIIB complex'''
+===Crystal structure of Mlc/EIIB complex===
-==Overview==
+<!--
-In Escherichia coli, glucose-dependent transcriptional induction of genes encoding a variety of sugar-metabolizing enzymes and transport systems is mediated by the phosphorylation state-dependent interaction of membrane-bound enzyme IICB(Glc) (EIICB(Glc)) with the global repressor Mlc. Here we report the crystal structure of a tetrameric Mlc in a complex with four molecules of enzyme IIB(Glc) (EIIB), the cytoplasmic domain of EIICB(Glc). Each monomer of Mlc has one bound EIIB molecule, indicating the 1:1 stoichiometry. The detailed view of the interface, along with the high-resolution structure of EIIB containing a sulfate ion at the phosphorylation site, suggests that the phosphorylation-induced steric hindrance and disturbance of polar intermolecular interactions impede complex formation. Furthermore, we reveal that Mlc possesses a built-in flexibility for the structural adaptation to its target DNA and that interaction of Mlc with EIIB fused only to dimeric proteins resulted in the loss of its DNA binding ability, suggesting that flexibility of the Mlc structure is indispensable for its DNA binding.
+The line below this paragraph, {{ABSTRACT_PUBMED_18319344}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18319344 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18319344}}
 ==About this Structure==
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 [[Category: Transmembrane]]
 [[Category: Transport]]
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