1qyn

From Proteopedia

(Difference between revisions)

Current revision

Crystal Structure of SecB from Escherichia coli

Structural highlights

1qyn is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.35Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SECB_ECOLI One of the proteins required for the normal export of some 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. Its substrates include AmpC, DegP, FhuA, FkpA, GBP, LamB, MalE (MBP), OmpA, OmpF, OmpT, OmpX, OppA, PhoE, TolB, TolC, YbgF, YcgK, YgiW and YncE.[HAMAP-Rule:MF_00821]

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

The chaperone SecB from Escherichia coli is primarily involved in passing precursor proteins into the Sec system via specific interactions with SecA. The crystal structure of SecB from E. coli has been solved to 2.35 A resolution. The structure shows flexibility in the crossover loop and the helix-connecting loop, regions that have been implicated to be part of the SecB substrate-binding site. Moreover conformational variability of Trp36 is observed as well as different loop conformations for the different monomers. Based on this, we speculate that SecB can regulate the access or extent of its hydrophobic substrate-binding site, by modulating the conformation of the crossover loop and the helix-connecting loop. The structure also clearly explains why the tetrameric equilibrium is shifted towards the dimeric state in the mutant SecBCys76Tyr. The buried cysteine residue is crucial for tight packing, and mutations are likely to disrupt the tetramer formation but not the dimer formation.

Crystal structure of SecB from Escherichia coli.,Dekker C, de Kruijff B, Gros P J Struct Biol. 2003 Dec;144(3):313-9. PMID:14643199^[1]

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

References

↑ Dekker C, de Kruijff B, Gros P. Crystal structure of SecB from Escherichia coli. J Struct Biol. 2003 Dec;144(3):313-9. PMID:14643199

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/1qyn"

Categories: Escherichia coli | Large Structures | Dekker C | Gros P | De Kruijff B

@@ Line 1: / Line 1: @@
 ==Crystal Structure of SecB from Escherichia coli==
-<StructureSection load='1qyn' size='340' side='right' caption='[[1qyn]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
+<StructureSection load='1qyn' size='340' side='right'caption='[[1qyn]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1qyn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QYN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QYN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1qyn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QYN FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SECB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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]] 2.35&#8491;</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=1qyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qyn OCA], [http://pdbe.org/1qyn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qyn RCSB], [http://www.ebi.ac.uk/pdbsum/1qyn PDBsum]</span></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=1qyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qyn OCA], [https://pdbe.org/1qyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qyn RCSB], [https://www.ebi.ac.uk/pdbsum/1qyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qyn ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SECB_ECOLI SECB_ECOLI]] One of the proteins required for the normal export of some 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. Its substrates include AmpC, DegP, FhuA, FkpA, GBP, LamB, MalE (MBP), OmpA, OmpF, OmpT, OmpX, OppA, PhoE, TolB, TolC, YbgF, YcgK, YgiW and YncE.[HAMAP-Rule:MF_00821]
+[https://www.uniprot.org/uniprot/SECB_ECOLI SECB_ECOLI] One of the proteins required for the normal export of some 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. Its substrates include AmpC, DegP, FhuA, FkpA, GBP, LamB, MalE (MBP), OmpA, OmpF, OmpT, OmpX, OppA, PhoE, TolB, TolC, YbgF, YcgK, YgiW and YncE.[HAMAP-Rule:MF_00821]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qy/1qyn_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qy/1qyn_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 31: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
-[[Category: Dekker, C]]
+[[Category: Large Structures]]
-[[Category: Gros, P]]
+[[Category: Dekker C]]
-[[Category: Kruijff, B de]]
+[[Category: Gros P]]
-[[Category: Chaperone]]
+[[Category: De Kruijff B]]
-[[Category: Greek key beta sheet]]
-[[Category: Tetramer]]

1qyn

From Proteopedia

Current revision

Crystal Structure of SecB from Escherichia coli

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox