2kxx: Difference between revisions
New page: '''Unreleased structure''' The entry 2kxx is ON HOLD Authors: Kim, K., Okon, M., Escobar, E., Kang, H., McIntosh, L., Paetzel, M. Description: NMR Structure of an E. coli lipoprotein ... |
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==NMR Structure of Escherichia coli BamE, a Lipoprotein Component of the beta-Barrel Assembly Machinery Complex== | |||
<StructureSection load='2kxx' size='340' side='right'caption='[[2kxx]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2kxx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KXX FirstGlance]. <br> | |||
</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=2kxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kxx OCA], [https://pdbe.org/2kxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kxx RCSB], [https://www.ebi.ac.uk/pdbsum/2kxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kxx ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/BAME_ECOLI BAME_ECOLI] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. May modulate the conformation of BamA, likely through interactions with BamD.<ref>PMID:17404237</ref> <ref>PMID:20378773</ref> <ref>PMID:21823654</ref> <ref>PMID:22178970</ref> <ref>PMID:21207987</ref> <ref>PMID:21586578</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In Escherichia coli, the BAM complex catalyzes the essential process of assembling outer membrane proteins (OMPs). This complex consists of five proteins: one membrane-bound protein, BamA, and four lipoproteins, BamB, BamC, BamD, and BamE. Despite their importance in OMP biogenesis, there is currently a lack of functional and structural information on the BAM complex lipoproteins. BamE is the smallest but most conserved lipoprotein in the complex. The structural and dynamic properties of monomeric BamE (residues 21-133) were determined by NMR spectroscopy. The protein folds as two alpha-helices packed against a three-stranded antiparallel beta-sheet. The N-terminal (Ser21-Thr39) and C-terminal (Pro108-Asn113) residues, as well as a beta-hairpin loop (Val76-Gln89), are highly flexible on the subnanosecond time scale. BamE expressed and purified from E. coli also exists in a kinetically trapped dimeric state that has dramatically different NMR spectra, and hence structural features, relative to its monomeric form. The functional significance of the BamE dimer remains to be established. Structural comparison to proteins with a similar architecture suggests that BamE may play a role in mediating the association of the BAM complex or with the BAM complex substrates. | |||
Structural Characterization of Escherichia coli BamE, a Lipoprotein Component of the beta-Barrel Assembly Machinery Complex.,Kim KH, Kang HS, Okon M, Escobar-Cabrera E, McIntosh LP, Paetzel M Biochemistry. 2011 Feb 15;50(6):1081-90. Epub 2011 Jan 24. PMID:21207987<ref>PMID:21207987</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2kxx" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Bam complex 3D structures|Bam complex 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Escobar E]] | |||
[[Category: Kang H]] | |||
[[Category: Kim K]] | |||
[[Category: McIntosh L]] | |||
[[Category: Okon M]] | |||
[[Category: Paetzel M]] | |||
Latest revision as of 08:37, 15 May 2024
NMR Structure of Escherichia coli BamE, a Lipoprotein Component of the beta-Barrel Assembly Machinery ComplexNMR Structure of Escherichia coli BamE, a Lipoprotein Component of the beta-Barrel Assembly Machinery Complex
Structural highlights
FunctionBAME_ECOLI Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. May modulate the conformation of BamA, likely through interactions with BamD.[1] [2] [3] [4] [5] [6] Publication Abstract from PubMedIn Escherichia coli, the BAM complex catalyzes the essential process of assembling outer membrane proteins (OMPs). This complex consists of five proteins: one membrane-bound protein, BamA, and four lipoproteins, BamB, BamC, BamD, and BamE. Despite their importance in OMP biogenesis, there is currently a lack of functional and structural information on the BAM complex lipoproteins. BamE is the smallest but most conserved lipoprotein in the complex. The structural and dynamic properties of monomeric BamE (residues 21-133) were determined by NMR spectroscopy. The protein folds as two alpha-helices packed against a three-stranded antiparallel beta-sheet. The N-terminal (Ser21-Thr39) and C-terminal (Pro108-Asn113) residues, as well as a beta-hairpin loop (Val76-Gln89), are highly flexible on the subnanosecond time scale. BamE expressed and purified from E. coli also exists in a kinetically trapped dimeric state that has dramatically different NMR spectra, and hence structural features, relative to its monomeric form. The functional significance of the BamE dimer remains to be established. Structural comparison to proteins with a similar architecture suggests that BamE may play a role in mediating the association of the BAM complex or with the BAM complex substrates. Structural Characterization of Escherichia coli BamE, a Lipoprotein Component of the beta-Barrel Assembly Machinery Complex.,Kim KH, Kang HS, Okon M, Escobar-Cabrera E, McIntosh LP, Paetzel M Biochemistry. 2011 Feb 15;50(6):1081-90. Epub 2011 Jan 24. PMID:21207987[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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