1u2m: Difference between revisions

Latest revision as of 08:46, 1 May 2024

Crystal Structure of Skp

Structural highlights

1u2m is a 3 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 2.3Å
Ligands:	MSE
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SKP_ECOLI Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm. Required for the efficient release of OmpA from the inner membrane, the maintenance of its solubility in the periplasm, and, in association with lipopolysaccharide (LPS), for the efficient folding and insertion of OmpA into the outer membrane.^[1] ^[2] ^[3] ^[4] ^[5]

Evolutionary Conservation

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

References

↑ Chen R, Henning U. A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins. Mol Microbiol. 1996 Mar;19(6):1287-94. PMID:8730870
↑ De Cock H, Schafer U, Potgeter M, Demel R, Muller M, Tommassen J. Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of Skp in the biogenesis of outer membrane protein. Eur J Biochem. 1999 Jan;259(1-2):96-103. PMID:9914480
↑ Schafer U, Beck K, Muller M. Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins. J Biol Chem. 1999 Aug 27;274(35):24567-74. PMID:10455120
↑ Harms N, Koningstein G, Dontje W, Muller M, Oudega B, Luirink J, de Cock H. The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane. J Biol Chem. 2001 Jun 1;276(22):18804-11. Epub 2001 Mar 5. PMID:11278858 doi:https://dx.doi.org/10.1074/jbc.M011194200
↑ Bulieris PV, Behrens S, Holst O, Kleinschmidt JH. Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide. J Biol Chem. 2003 Mar 14;278(11):9092-9. Epub 2002 Dec 30. PMID:12509434 doi:https://dx.doi.org/10.1074/jbc.M211177200

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Chen R, Henning U. A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins. Mol Microbiol. 1996 Mar;19(6):1287-94. PMID:8730870

[2] De Cock H, Schafer U, Potgeter M, Demel R, Muller M, Tommassen J. Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of Skp in the biogenesis of outer membrane protein. Eur J Biochem. 1999 Jan;259(1-2):96-103. PMID:9914480

[3] Schafer U, Beck K, Muller M. Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins. J Biol Chem. 1999 Aug 27;274(35):24567-74. PMID:10455120

[4] Harms N, Koningstein G, Dontje W, Muller M, Oudega B, Luirink J, de Cock H. The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane. J Biol Chem. 2001 Jun 1;276(22):18804-11. Epub 2001 Mar 5. PMID:11278858 doi:https://dx.doi.org/10.1074/jbc.M011194200

[5] Bulieris PV, Behrens S, Holst O, Kleinschmidt JH. Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide. J Biol Chem. 2003 Mar 14;278(11):9092-9. Epub 2002 Dec 30. PMID:12509434 doi:https://dx.doi.org/10.1074/jbc.M211177200

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[2]

[3]

[4]

[5]

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1u2m.png|left|200px]]
-<!--
+==Crystal Structure of Skp==
-The line below this paragraph, containing "STRUCTURE_1u2m", creates the "Structure Box" on the page.
+<StructureSection load='1u2m' size='340' side='right'caption='[[1u2m]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1u2m]] is a 3 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=1U2M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U2M FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-{{STRUCTURE_1u2m|  PDB=1u2m  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1u2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u2m OCA], [https://pdbe.org/1u2m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u2m RCSB], [https://www.ebi.ac.uk/pdbsum/1u2m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u2m ProSAT]</span></td></tr>
+</table>
-===Crystal Structure of Skp===
+== Function ==
+[https://www.uniprot.org/uniprot/SKP_ECOLI SKP_ECOLI] Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm. Required for the efficient release of OmpA from the inner membrane, the maintenance of its solubility in the periplasm, and, in association with lipopolysaccharide (LPS), for the efficient folding and insertion of OmpA into the outer membrane.<ref>PMID:8730870</ref> <ref>PMID:9914480</ref> <ref>PMID:10455120</ref> <ref>PMID:11278858</ref> <ref>PMID:12509434</ref>
+== Evolutionary Conservation ==
-<!--
+[[Image:Consurf_key_small.gif|200px|right]]
-The line below this paragraph, {{ABSTRACT_PUBMED_15304217}}, adds the Publication Abstract to the page
+Check<jmol>
-(as it appears on PubMed at http://www.pubmed.gov), where 15304217 is the PubMed ID number.
+  <jmolCheckbox>
--->
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u2/1u2m_consurf.spt"</scriptWhenChecked>
-{{ABSTRACT_PUBMED_15304217}}
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
-==About this Structure==
+  </jmolCheckbox>
-U2M is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U2M OCA].
+</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=1u2m ConSurf].
+<div style="clear:both"></div>
-==Reference==
+== References ==
-<ref group="xtra">PMID:15304217</ref><references group="xtra"/>
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Sousa, M C.]]
+[[Category: Large Structures]]
-[[Category: Walton, T A.]]
+[[Category: Sousa MC]]
-[[Category: Chaperone]]
+[[Category: Walton TA]]
-[[Category: Coiled coil]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 02:30:41 2009''

1u2m: Difference between revisions

Latest revision as of 08:46, 1 May 2024

Crystal Structure of Skp

Structural highlights

Function

Evolutionary Conservation

References

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