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1bp1

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[[Image:1bp1.gif|left|200px]]<br />
 
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<applet load="1bp1" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1bp1, resolution 2.40&Aring;" />
 
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'''CRYSTAL STRUCTURE OF BPI, THE HUMAN BACTERICIDAL PERMEABILITY-INCREASING PROTEIN'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF BPI, THE HUMAN BACTERICIDAL PERMEABILITY-INCREASING PROTEIN==
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Bactericidal/permeability-increasing protein (BPI), a potent antimicrobial, protein of 456 residues, binds to and neutralizes lipopolysaccharides from, the outer membrane of Gram-negative bacteria. At a resolution of 2.4, angstroms, the crystal structure of human BPI shows a boomerang-shaped, molecule formed by two similar domains. Two apolar pockets on the concave, surface of the boomerang each bind a molecule of phosphatidylcholine, primarily by interacting with their acyl chains; this suggests that the, pockets may also bind the acyl chains of lipopolysaccharide. As a model, for the related plasma lipid transfer proteins, BPI illuminates a, mechanism of lipid transfer for this protein family.
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<StructureSection load='1bp1' size='340' side='right'caption='[[1bp1]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1bp1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BP1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BP1 FirstGlance]. <br>
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1BP1 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with PC1 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Sites: C and N. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BP1 OCA]].
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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]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PC1:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PC1</scene></td></tr>
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==Reference==
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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=1bp1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bp1 OCA], [https://pdbe.org/1bp1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bp1 RCSB], [https://www.ebi.ac.uk/pdbsum/1bp1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bp1 ProSAT]</span></td></tr>
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Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution., Beamer LJ, Carroll SF, Eisenberg D, Science. 1997 Jun 20;276(5320):1861-4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9188532 9188532]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BPI_HUMAN BPI_HUMAN] The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa.<ref>PMID:2722846</ref> <ref>PMID:1937776</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bp/1bp1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1bp1 ConSurf].
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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: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Beamer, L.J.]]
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[[Category: Beamer LJ]]
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[[Category: Carroll, S.F.]]
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[[Category: Carroll SF]]
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[[Category: Eisenberg, D.]]
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[[Category: Eisenberg D]]
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[[Category: PC1]]
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[[Category: antibiotic]]
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[[Category: bactericidal]]
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[[Category: lipid-binding]]
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[[Category: lipopolysaccharide-binding]]
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[[Category: permeability-increasing]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:40:27 2007''
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Current revision

CRYSTAL STRUCTURE OF BPI, THE HUMAN BACTERICIDAL PERMEABILITY-INCREASING PROTEIN

PDB ID 1bp1

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