2jmm
From Proteopedia
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| - | [[Image:2jmm.jpg|left|200px]] | + | [[Image:2jmm.jpg|left|200px]] |
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| - | '''NMR solution structure of a minimal transmembrane beta-barrel platform protein''' | + | {{Structure |
| + | |PDB= 2jmm |SIZE=350|CAPTION= <scene name='initialview01'>2jmm</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= ompA, con, tolG, tut ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''NMR solution structure of a minimal transmembrane beta-barrel platform protein''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2JMM is a [ | + | 2JMM is a [[Protein complex]] 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=2JMM OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17260943 17260943] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: membrane protein]] | [[Category: membrane protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:42:59 2008'' |
Revision as of 15:43, 20 March 2008
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| Gene: | ompA, con, tolG, tut (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR solution structure of a minimal transmembrane beta-barrel platform protein
Overview
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.
About this Structure
2JMM is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 17:42:59 2008
