1qwd
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(New page: 200px<br /><applet load="1qwd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qwd, resolution 1.75Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 22:56, 20 November 2007
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CRYSTAL STRUCTURE OF A BACTERIAL LIPOCALIN, THE BLC GENE PRODUCT FROM E. COLI
Overview
Lipocalins form a large multifunctional family of small proteins (15-25, kDa) first discovered in eukaryotes. More recently, several types of, bacterial lipocalins have been reported, among which Blc from Escherichia, coli is an outer membrane lipoprotein. As part of our structural genomics, effort on proteins from E. coli, we have expressed, crystallized and, solved the structure of Blc at 1.8 A resolution using remote SAD with, xenon. The structure of Blc, the first of a bacterial lipocalin, exhibits, a classical fold formed by a beta-barrel and a alpha-helix similar to that, of the moth bilin binding protein. Its empty and open cavity, however, is, too narrow to accommodate bilin, while the alkyl chains of two fatty acids, or of a phospholipid could be readily modeled inside the cavity. Blc was, reported to be expressed under stress conditions such as starvation or, high osmolarity, during which the cell envelope suffers and requires, maintenance. These data, together with our structural interpretation, suggest a role for Blc in storage or transport of lipids necessary for, membrane repair or maintenance.
About this Structure
1QWD is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The crystal structure of the Escherichia coli lipocalin Blc suggests a possible role in phospholipid binding., Campanacci V, Nurizzo D, Spinelli S, Valencia C, Tegoni M, Cambillau C, FEBS Lett. 2004 Mar 26;562(1-3):183-8. PMID:15044022
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