3mbt

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[[Image:3mbt.png|left|200px]]
 
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==Structure of monomeric Blc from E. coli==
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The line below this paragraph, containing "STRUCTURE_3mbt", creates the "Structure Box" on the page.
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<StructureSection load='3mbt' size='340' side='right'caption='[[3mbt]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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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'>[[3mbt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MBT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MBT FirstGlance]. <br>
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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]] 2.6&#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=3mbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mbt OCA], [https://pdbe.org/3mbt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mbt RCSB], [https://www.ebi.ac.uk/pdbsum/3mbt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mbt ProSAT]</span></td></tr>
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{{STRUCTURE_3mbt| PDB=3mbt | SCENE= }}
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</table>
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== Function ==
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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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The first bacterial member of the lipocalin protein family, Blc, was identified in Escherichia coli as an outer membrane lipoprotein that is expressed under conditions of environmental stress. Previous crystallographic studies in space group P222 with two molecules per asymmetric unit, supported by static light-scattering experiments in solution, indicated that Blc may form a functional homodimer with lysophospholipid binding activity. Here, a new crystal structure of recombinant Blc in space group I422 with one molecule in the asymmetric unit is described. The crystal packing differs considerably from that observed previously, which was determined using an N-terminally extended version of Blc dubbed `Blc-X'. In particular, the characteristic large interface region that was previously described as being responsible for stable dimer formation is absent in the I422 crystal structure. Thus, the dimerization behaviour of Blc-X was most likely to be caused by the additional N-terminal peptide segment resulting from the cloning strategy employed. In contrast, we used a native-like N-terminus for Blc with just the lipid-anchored first Cys residue replaced by Ala. The fully monomeric status of this recombinant version of Blc in solution was confirmed by size-exclusion chromatography as well as analytical ultracentrifugation. Consequently, these data shed new light on the previously postulated lipid-binding mechanism and biological role of Blc. Beyond this, our findings illustrate that cloning artefacts, which frequently result from recombinant protein production for structural studies, must be considered with special caution when interpreting oligomerization and/or conformational effects.
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===Structure of monomeric Blc from E. coli===
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Structural and biochemical analyses reveal a monomeric state of the bacterial lipocalin Blc.,Schiefner A, Chatwell L, Breustedt DA, Skerra A Acta Crystallogr D Biol Crystallogr. 2010 Dec;66(Pt 12):1308-15. Epub 2010, Nov 16. PMID:21123871<ref>PMID:21123871</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3mbt" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 21123871 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_21123871}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia coli K-12]]
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[[3mbt]] is a 1 chain structure with 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=3MBT OCA].
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[[Category: Large Structures]]
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[[Category: Schiefner A]]
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==Reference==
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[[Category: Skerra A]]
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<ref group="xtra">PMID:021123871</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
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[[Category: Schiefner, A.]]
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[[Category: Skerra, A.]]
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[[Category: Bacterial outer membrane lipoprotein]]
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[[Category: Beta-barrel]]
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[[Category: Lipid binding protein]]
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[[Category: Lipid membrane anchor]]
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[[Category: Lipocalin]]
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[[Category: Membrane protein]]
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Current revision

Structure of monomeric Blc from E. coli

PDB ID 3mbt

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