This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4n75

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 05:04, 25 August 2022

Structural Basis of BamA-mediate Outer Membrane Protein Biogenesis

Structural highlights

4n75 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	4n74
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

Publication Abstract from PubMed

In gram-negative bacteria, the assembly of outer membrane proteins (OMPs) requires a beta-barrel assembly machinery (BAM) complex, of which BamA is an essential and evolutionarily conserved component. To elucidate the mechanism of BamA-mediated OMP biogenesis, we determined the crystal structure of the C-terminal transmembrane domain of BamA from Escherichia coli (EcBamA) at 2.6 A resolution. The structure reveals 2 distinct features. First, a portion of the extracellular side of the beta barrel is composed of 5 markedly short beta strands, and the loops stemming from these beta strands form a potential surface cavity, filled by a portion of the L6 loop that includes the conserved VRGF/Y motif found in the Omp85 family. Second, the 4 extracellular loops L3, L4, L6, and L7 of EcBamA form a dome over the barrel, stabilized by a salt-bridge interaction network. Functional data show that hydrophilic-to-hydrophobic mutations of the potential hydrophilic surface cavity and a single Arg547Ala point mutation that may destabilize the dome severely affect the function of EcBamA. Our structure of the EcBamA beta barrel and structure-based mutagenesis studies suggest that the transmembrane beta strands of OMP substrates may integrate into the outer membrane at the interface of the first and last beta strands of the EcBamA barrel, whereas the soluble loops or domains may be transported out of the cell via the hydrophilic surface cavity on dislocation of the VRGF/Y motif of L6. In addition, the dome over the barrel may play an important role in maintaining the efficiency of OMP biogenesis.-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.

Structural and functional analysis of the beta-barrel domain of BamA from Escherichia coli.,Ni D, Wang Y, Yang X, Zhou H, Hou X, Cao B, Lu Z, Zhao X, Yang K, Huang Y FASEB J. 2014 Mar 11. PMID:24619089^[6]

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

References

↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4n75"

@@ Line 3: / Line 3: @@
 <StructureSection load='4n75' size='340' side='right'caption='[[4n75]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4n75]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N75 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N75 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4n75]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N75 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N75 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n74|4n74]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4n74|4n74]]</div></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=4n75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n75 OCA], [http://pdbe.org/4n75 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n75 RCSB], [http://www.ebi.ac.uk/pdbsum/4n75 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n75 ProSAT]</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=4n75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n75 OCA], [https://pdbe.org/4n75 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n75 RCSB], [https://www.ebi.ac.uk/pdbsum/4n75 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n75 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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>
+[[https://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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 26: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Ecoli]]
 [[Category: Large Structures]]
 [[Category: Ni, D C]]

4n75

From Proteopedia

Revision as of 05:04, 25 August 2022

Structural Basis of BamA-mediate Outer Membrane Protein Biogenesis

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox