1qwd

<table><tr><td colspan='2'>[[1qwd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1QWD FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BLC OR B4149 OR Z5756 OR ECS5130 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1qwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwd OCA], [http://pdbe.org/1qwd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qwd RCSB], [http://www.ebi.ac.uk/pdbsum/1qwd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qwd ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/BLC_ECOLI BLC_ECOLI]] Involved in the storage or transport of lipids necessary for membrane maintenance under stressful conditions. Displays a binding preference for lysophospholipids.<ref>PMID:15044022</ref>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:15044022</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1qwd" style="background-color:#fffaf0;"></div>

[[Category: Bacillus coli migula 1895]]

[[Category: Cambillau, C]]

[[Category: Campanacci, V]]

[[Category: Nurizzo, D]]

[[Category: Spinelli, S]]

[[Category: Valencia, C]]

[[Category: Lipid binding protein]]