2mhk

From Proteopedia

(Difference between revisions)

Current revision

E. coli LpoA N-terminal domain

Structural highlights

2mhk is a 1 chain structure with sequence from Escherichia coli K-12. 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

LPOA_ECOLI Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1A (PBP1a). Stimulates transpeptidase activity of PBP1a in vitro.^[1] ^[2]

Publication Abstract from PubMed

The bacterial cell envelope contains the stress-bearing peptidoglycan layer, which is enlarged during cell growth and division by membrane-anchored synthases guided by cytoskeletal elements. In Escherichia coli, the major peptidoglycan synthase PBP1A requires stimulation by the outer-membrane-anchored lipoprotein LpoA. Whereas the C-terminal domain of LpoA interacts with PBP1A to stimulate its peptide crosslinking activity, little is known about the role of the N-terminal domain. Herein we report its NMR structure, which adopts an all-alpha-helical fold comprising a series of helix-turn-helix tetratricopeptide-repeat (TPR)-like motifs. NMR spectroscopy of full-length LpoA revealed two extended flexible regions in the C-terminal domain and limited, if any, flexibility between the N- and C-terminal domains. Analytical ultracentrifugation and small-angle X-ray scattering results are consistent with LpoA adopting an elongated shape, with dimensions sufficient to span from the outer membrane through the periplasm to interact with the peptidoglycan synthase PBP1A.

Elongated Structure of the Outer-Membrane Activator of Peptidoglycan Synthesis LpoA: Implications for PBP1A Stimulation.,Jean NL, Bougault CM, Lodge A, Derouaux A, Callens G, Egan AJ, Ayala I, Lewis RJ, Vollmer W, Simorre JP Structure. 2014 Jul 8;22(7):1047-54. doi: 10.1016/j.str.2014.04.017. Epub 2014, Jun 19. PMID:24954617^[3]

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

References

↑ Typas A, Banzhaf M, van den Berg van Saparoea B, Verheul J, Biboy J, Nichols RJ, Zietek M, Beilharz K, Kannenberg K, von Rechenberg M, Breukink E, den Blaauwen T, Gross CA, Vollmer W. Regulation of peptidoglycan synthesis by outer-membrane proteins. Cell. 2010 Dec 23;143(7):1097-109. doi: 10.1016/j.cell.2010.11.038. PMID:21183073 doi:http://dx.doi.org/10.1016/j.cell.2010.11.038
↑ Paradis-Bleau C, Markovski M, Uehara T, Lupoli TJ, Walker S, Kahne DE, Bernhardt TG. Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases. Cell. 2010 Dec 23;143(7):1110-20. doi: 10.1016/j.cell.2010.11.037. PMID:21183074 doi:http://dx.doi.org/10.1016/j.cell.2010.11.037
↑ Jean NL, Bougault CM, Lodge A, Derouaux A, Callens G, Egan AJ, Ayala I, Lewis RJ, Vollmer W, Simorre JP. Elongated Structure of the Outer-Membrane Activator of Peptidoglycan Synthesis LpoA: Implications for PBP1A Stimulation. Structure. 2014 Jul 8;22(7):1047-54. doi: 10.1016/j.str.2014.04.017. Epub 2014, Jun 19. PMID:24954617 doi:http://dx.doi.org/10.1016/j.str.2014.04.017

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 2mhk is ON HOLD  until Paper Publication
+==E. coli LpoA N-terminal domain==
+<StructureSection load='2mhk' size='340' side='right'caption='[[2mhk]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2mhk]] 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=2MHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MHK 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=2mhk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mhk OCA], [https://pdbe.org/2mhk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mhk RCSB], [https://www.ebi.ac.uk/pdbsum/2mhk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mhk ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LPOA_ECOLI LPOA_ECOLI] Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1A (PBP1a). Stimulates transpeptidase activity of PBP1a in vitro.<ref>PMID:21183073</ref> <ref>PMID:21183074</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The bacterial cell envelope contains the stress-bearing peptidoglycan layer, which is enlarged during cell growth and division by membrane-anchored synthases guided by cytoskeletal elements. In Escherichia coli, the major peptidoglycan synthase PBP1A requires stimulation by the outer-membrane-anchored lipoprotein LpoA. Whereas the C-terminal domain of LpoA interacts with PBP1A to stimulate its peptide crosslinking activity, little is known about the role of the N-terminal domain. Herein we report its NMR structure, which adopts an all-alpha-helical fold comprising a series of helix-turn-helix tetratricopeptide-repeat (TPR)-like motifs. NMR spectroscopy of full-length LpoA revealed two extended flexible regions in the C-terminal domain and limited, if any, flexibility between the N- and C-terminal domains. Analytical ultracentrifugation and small-angle X-ray scattering results are consistent with LpoA adopting an elongated shape, with dimensions sufficient to span from the outer membrane through the periplasm to interact with the peptidoglycan synthase PBP1A.
-Authors: Jean, N.L., Bougault, C., Lodge, A., Derouaux, A., Callens, G., Egan, A., Lewis, R.J., Vollmer, W., Simorre, J.
+Elongated Structure of the Outer-Membrane Activator of Peptidoglycan Synthesis LpoA: Implications for PBP1A Stimulation.,Jean NL, Bougault CM, Lodge A, Derouaux A, Callens G, Egan AJ, Ayala I, Lewis RJ, Vollmer W, Simorre JP Structure. 2014 Jul 8;22(7):1047-54. doi: 10.1016/j.str.2014.04.017. Epub 2014, Jun 19. PMID:24954617<ref>PMID:24954617</ref>
-Description: E. coli LpoA N-terminal domain
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2mhk" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia coli K-12]]
+[[Category: Large Structures]]
+[[Category: Bougault C]]
+[[Category: Callens G]]
+[[Category: Derouaux A]]
+[[Category: Egan A]]
+[[Category: Jean NL]]
+[[Category: Lewis RJ]]
+[[Category: Lodge A]]
+[[Category: Simorre J]]
+[[Category: Vollmer W]]

2mhk

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Current revision

E. coli LpoA N-terminal domain

Structural highlights

Function

Publication Abstract from PubMed

References

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