1ozb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:04, 14 February 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='1ozb' size='340' side='right'caption='[[1ozb]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='1ozb' size='340' side='right'caption='[[1ozb]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1ozb]] is a 10 chain structure with sequence from [http://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=1OZB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1OZB FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1ozb]] is a 10 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=1OZB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OZB FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 2.8&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fx3|1fx3]], [[1m6n|1m6n]], [[1nl3|1nl3]]</div></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=1ozb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ozb OCA], [https://pdbe.org/1ozb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ozb RCSB], [https://www.ebi.ac.uk/pdbsum/1ozb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ozb ProSAT]</span></td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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>
</table>
== Function ==
== Function ==
-
[[http://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. [[http://www.uniprot.org/uniprot/SECA_HAEIN 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]
+
[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]]
Line 21: Line 20:
</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=1ozb 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=1ozb ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
-
<div style="background-color:#fffaf0;">
 
-
== 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<ref>PMID:14517549</ref>
 
- 
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
-
</div>
 
-
<div class="pdbe-citations 1ozb" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
-
*[[Preprotein translocase|Preprotein translocase]]
+
*[[Preprotein translocase 3D structures|Preprotein translocase 3D structures]]
*[[SecA|SecA]]
*[[SecA|SecA]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Bacterium influenzae lehmann and neumann 1896]]
+
[[Category: Haemophilus influenzae]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Xu, Z]]
+
[[Category: Xu Z]]
-
[[Category: Zhou, J]]
+
[[Category: Zhou J]]
-
[[Category: Protein transport]]
+
-
[[Category: Protein-protein complex]]
+
-
[[Category: Zinc binding motif]]
+

Current revision

Crystal Structure of SecB complexed with SecA C-terminus

PDB ID 1ozb

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools