2jmm

From Proteopedia

(Difference between revisions)

Revision as of 10:07, 20 December 2023

NMR solution structure of a minimal transmembrane beta-barrel platform protein

Structural highlights

2jmm is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

OMPA_ECOLI Required for the action of colicins K and L and for the stabilization of mating aggregates in conjugation. Serves as a receptor for a number of T-even like phages. Also acts as a porin with low permeability that allows slow penetration of small solutes.

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

In this study, we were concerned with the structural role of the surface-exposed extracellular loops of the N-terminal transmembrane (TM) domain of OmpA. A variant of the TM domain of outer membrane protein A (OmpA) with all four such loops shortened, which we call the beta-barrel platform (BBP), was successfully refolded. This indicates that the removed parts of the surface-exposed loops indeed do not contain amino acid sequences critical for this membrane protein's refolding in vitro. BBP has the potential to be used as a template beta-barrel membrane protein structure for the development of novel functions, although our results also highlight the potential difficulties that can arise when functionality is being engineered into the loop regions of membrane proteins. We have used solution nuclear magnetic resonance spectroscopy to determine the global fold of BBP+EF, BBP with a metal ion-binding EF-hand inserted in one of the shortened loops. BBP and BBP+EF in dihexanoylphosphatidylcholine micelles are eight-stranded antiparallel beta-barrels, and BBP represents the smallest beta-structured integral membrane protein known to date.

A minimal transmembrane beta-barrel platform protein studied by nuclear magnetic resonance.,Johansson MU, Alioth S, Hu K, Walser R, Koebnik R, Pervushin K Biochemistry. 2007 Feb 6;46(5):1128-40. PMID:17260943^[1]

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

References

↑ Johansson MU, Alioth S, Hu K, Walser R, Koebnik R, Pervushin K. A minimal transmembrane beta-barrel platform protein studied by nuclear magnetic resonance. Biochemistry. 2007 Feb 6;46(5):1128-40. PMID:17260943 doi:10.1021/bi061265e

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2jmm"

@@ Line 1: / Line 1: @@
 ==NMR solution structure of a minimal transmembrane beta-barrel platform protein==
-<StructureSection load='2jmm' size='340' side='right'caption='[[2jmm]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='2jmm' size='340' side='right'caption='[[2jmm]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2jmm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JMM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2jmm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JMM FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ompA, con, tolG, tut ([https://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">Solution NMR</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=2jmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jmm OCA], [https://pdbe.org/2jmm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jmm RCSB], [https://www.ebi.ac.uk/pdbsum/2jmm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jmm ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/OMPA_ECOLI OMPA_ECOLI]] Required for the action of colicins K and L and for the stabilization of mating aggregates in conjugation. Serves as a receptor for a number of T-even like phages. Also acts as a porin with low permeability that allows slow penetration of small solutes.
+[https://www.uniprot.org/uniprot/OMPA_ECOLI OMPA_ECOLI] Required for the action of colicins K and L and for the stabilization of mating aggregates in conjugation. Serves as a receptor for a number of T-even like phages. Also acts as a porin with low permeability that allows slow penetration of small solutes.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Alioth, S]]
+[[Category: Alioth S]]
-[[Category: Hu, K]]
+[[Category: Hu K]]
-[[Category: Johansson, M U]]
+[[Category: Johansson MU]]
-[[Category: Koebnik, R]]
+[[Category: Koebnik R]]
-[[Category: Pervushin, K]]
+[[Category: Pervushin K]]
-[[Category: Walser, R]]
+[[Category: Walser R]]
-[[Category: Membrane protein]]

2jmm

From Proteopedia

Revision as of 10:07, 20 December 2023

NMR solution structure of a minimal transmembrane beta-barrel platform protein

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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