1fx3: Difference between revisions

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<StructureSection load='1fx3' size='340' side='right'caption='[[1fx3]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='1fx3' size='340' side='right'caption='[[1fx3]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1fx3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FX3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1fx3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FX3 FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fx3 OCA], [https://pdbe.org/1fx3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fx3 RCSB], [https://www.ebi.ac.uk/pdbsum/1fx3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fx3 ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fx3 OCA], [https://pdbe.org/1fx3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fx3 RCSB], [https://www.ebi.ac.uk/pdbsum/1fx3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fx3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/SECB_HAEIN SECB_HAEIN]] One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA.  
[https://www.uniprot.org/uniprot/SECB_HAEIN SECB_HAEIN] One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1fx3 ConSurf].
</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=1fx3 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
SecB is a bacterial molecular chaperone involved in mediating translocation of newly synthesized polypeptides across the cytoplasmic membrane of bacteria. The crystal structure of SecB from Haemophilus influenzae shows that the molecule is a tetramer organized as a dimer of dimers. Two long channels run along the side of the molecule. These are bounded by flexible loops and lined with conserved hydrophobic amino acids, which define a suitable environment for binding non-native polypeptides. The structure also reveals an acidic region on the top surface of the molecule, several residues of which have been implicated in binding to SecA, its downstream target.
Crystal structure of the bacterial protein export chaperone secB.,Xu Z, Knafels JD, Yoshino K Nat Struct Biol. 2000 Dec;7(12):1172-7. PMID:11101901<ref>PMID:11101901</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1fx3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacterium influenzae lehmann and neumann 1896]]
[[Category: Haemophilus influenzae]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Knafels, J D]]
[[Category: Knafels JD]]
[[Category: Xu, Z]]
[[Category: Xu Z]]
[[Category: Yoshino, K]]
[[Category: Yoshino K]]
[[Category: Protein trasnport]]
[[Category: Translocation]]
[[Category: Transport protein]]
Retrieved from "https://proteopedia.org/1fx3"