4n75

From Proteopedia

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'''Unreleased structure'''
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{{STRUCTURE_4n75| PDB=4n75 | SCENE= }}
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===Structural Basis of BamA-mediate Outer Membrane Protein Biogenesis===
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{{ABSTRACT_PUBMED_24619089}}
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The entry 4n75 is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/BAMA_ECOLI BAMA_ECOLI]] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery.<ref>PMID:15951436</ref> <ref>PMID:16102012</ref> <ref>PMID:16824102</ref> <ref>PMID:20378773</ref> <ref>PMID:21823654</ref>
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Authors: Ni, D.C.
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==About this Structure==
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[[4n75]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N75 OCA].
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Description: Structural Basis of BamA-mediate Outer Membrane Protein Biogenesis
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==Reference==
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<ref group="xtra">PMID:024619089</ref><references group="xtra"/><references/>
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[[Category: Ni, D C.]]
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[[Category: Barrel]]
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[[Category: Membrane protein]]
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[[Category: Omp85]]
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[[Category: Outer membrane protein biogenesis]]
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[[Category: Yaet]]

Revision as of 09:45, 16 April 2014

Template:STRUCTURE 4n75

Contents

Structural Basis of BamA-mediate Outer Membrane Protein Biogenesis

Template:ABSTRACT PUBMED 24619089

Function

[BAMA_ECOLI] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery.[1] [2] [3] [4] [5]

About this Structure

4n75 is a 2 chain structure. Full crystallographic information is available from OCA.

Reference

  • Ni D, Wang Y, Yang X, Zhou H, Hou X, Cao B, Lu Z, Zhao X, Yang K, Huang Y. Structural and functional analysis of the beta-barrel domain of BamA from Escherichia coli. FASEB J. 2014 Mar 11. PMID:24619089 doi:http://dx.doi.org/10.1096/fj.13-248450
  1. ↑ Doerrler WT, Raetz CR. Loss of outer membrane proteins without inhibition of lipid export in an Escherichia coli YaeT mutant. J Biol Chem. 2005 Jul 29;280(30):27679-87. Epub 2005 Jun 10. PMID:15951436 doi:http://dx.doi.org/M504796200
  2. ↑ Werner J, Misra R. YaeT (Omp85) affects the assembly of lipid-dependent and lipid-independent outer membrane proteins of Escherichia coli. Mol Microbiol. 2005 Sep;57(5):1450-9. PMID:16102012 doi:http://dx.doi.org/MMI4775
  3. ↑ Malinverni JC, Werner J, Kim S, Sklar JG, Kahne D, Misra R, Silhavy TJ. YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli. Mol Microbiol. 2006 Jul;61(1):151-64. PMID:16824102 doi:http://dx.doi.org/10.1111/j.1365-2958.2006.05211.x
  4. ↑ Hagan CL, Kim S, Kahne D. Reconstitution of outer membrane protein assembly from purified components. Science. 2010 May 14;328(5980):890-2. doi: 10.1126/science.1188919. Epub 2010 Apr, 8. PMID:20378773 doi:10.1126/science.1188919
  5. ↑ Hagan CL, Kahne D. The reconstituted Escherichia coli Bam complex catalyzes multiple rounds of beta-barrel assembly. Biochemistry. 2011 Sep 6;50(35):7444-6. doi: 10.1021/bi2010784. Epub 2011 Aug 11. PMID:21823654 doi:10.1021/bi2010784

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