1ozb

From Proteopedia

(Difference between revisions)

Revision as of 07:57, 15 February 2018

Crystal Structure of SecB complexed with SecA C-terminus

Structural highlights

1ozb is a 10 chain structure with sequence from "bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1fx3, 1m6n, 1nl3
Gene:	SECB OR HI0743 ("Bacterium influenzae" Lehmann and Neumann 1896), SECA OR HI0909 ("Bacterium influenzae" Lehmann and Neumann 1896)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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. [SECA_HAEIN] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane (By similarity).[HAMAP-Rule:MF_01382]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

SecB is a bacterial chaperone involved in directing pre-protein to the translocation pathway by its specific interaction with the peripheral membrane ATPase SecA. The SecB-binding site on SecA is located at its C terminus and consists of a stretch of highly conserved residues. The crystal structure of SecB in complex with the C-terminal 27 amino acids of SecA from Haemophilus influenzae shows that the SecA peptide is structured as a CCCH zinc-binding motif. One SecB tetramer is bound by two SecA peptides, and the interface involves primarily salt bridges and hydrogen bonding interactions. The structure explains the importance of the zinc-binding motif and conserved residues at the C terminus of SecA in its high-affinity binding with SecB. It also suggests a model of SecB-SecA interaction and its implication for the mechanism of pre-protein transfer in bacterial protein translocation.

Structural determinants of SecB recognition by SecA in bacterial protein translocation.,Zhou J, Xu Z Nat Struct Biol. 2003 Nov;10(11):942-7. Epub 2003 Sep 28. PMID:14517549^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zhou J, Xu Z. Structural determinants of SecB recognition by SecA in bacterial protein translocation. Nat Struct Biol. 2003 Nov;10(11):942-7. Epub 2003 Sep 28. PMID:14517549 doi:10.1038/nsb980

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ozb"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of SecB complexed with SecA C-terminus==
 <StructureSection load='1ozb' size='340' side='right' caption='[[1ozb]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fx3|1fx3]], [[1m6n|1m6n]], [[1nl3|1nl3]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SECB OR HI0743 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 "Bacterium influenzae" Lehmann and Neumann 1896]), SECA OR HI0909 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 "Bacterium influenzae" Lehmann and Neumann 1896])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ozb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ozb OCA], [http://pdbe.org/1ozb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ozb RCSB], [http://www.ebi.ac.uk/pdbsum/1ozb PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ozb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ozb OCA], [http://pdbe.org/1ozb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ozb RCSB], [http://www.ebi.ac.uk/pdbsum/1ozb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ozb ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oz/1ozb_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oz/1ozb_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1ozb" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Preprotein translocase|Preprotein translocase]]
-*[[SecA|SecA]]
 == References ==
 <references/>

1ozb

From Proteopedia

Revision as of 07:57, 15 February 2018

Crystal Structure of SecB complexed with SecA C-terminus

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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