1qwd

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[[Image:1qwd.gif|left|200px]]
 
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==CRYSTAL STRUCTURE OF A BACTERIAL LIPOCALIN, THE BLC GENE PRODUCT FROM E. COLI==
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The line below this paragraph, containing "STRUCTURE_1qwd", creates the "Structure Box" on the page.
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<StructureSection load='1qwd' size='340' side='right'caption='[[1qwd]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1qwd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1QWD FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwd OCA], [https://pdbe.org/1qwd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qwd RCSB], [https://www.ebi.ac.uk/pdbsum/1qwd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qwd ProSAT]</span></td></tr>
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{{STRUCTURE_1qwd| PDB=1qwd | SCENE= }}
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</table>
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== Function ==
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'''CRYSTAL STRUCTURE OF A BACTERIAL LIPOCALIN, THE BLC GENE PRODUCT FROM E. COLI'''
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[https://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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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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.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qw/1qwd_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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1QWD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWD OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qwd ConSurf].
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15044022 15044022]
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cambillau, C.]]
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[[Category: Cambillau C]]
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[[Category: Campanacci, V.]]
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[[Category: Campanacci V]]
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[[Category: Nurizzo, D.]]
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[[Category: Nurizzo D]]
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[[Category: Spinelli, S.]]
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[[Category: Spinelli S]]
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[[Category: Valencia, C.]]
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[[Category: Valencia C]]
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[[Category: Bacterial lipocalin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:46:37 2008''
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Current revision

CRYSTAL STRUCTURE OF A BACTERIAL LIPOCALIN, THE BLC GENE PRODUCT FROM E. COLI

PDB ID 1qwd

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