5vbg: Difference between revisions
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==Crystal Structure of full-length LpoA, Monoclinic form 1, from Haemophilus influenzae== | |||
<StructureSection load='5vbg' size='340' side='right' caption='[[5vbg]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5vbg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VBG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VBG FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kcn|5kcn]], [[5vat|5vat]]</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=5vbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vbg OCA], [http://pdbe.org/5vbg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vbg RCSB], [http://www.ebi.ac.uk/pdbsum/5vbg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vbg ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/LPOA_HAEIN LPOA_HAEIN]] Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1A (PBP1a). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In many Gram-negative bacteria, the peptidoglycan synthase PBP1A requires the outer membrane lipoprotein LpoA for constructing a functional peptidoglycan required for bacterial viability. Previously, we have shown that the C-terminal domain of Haemophilus influenzae LpoA (HiLpoA) has a highly conserved, putative substrate-binding cleft between two alpha/beta lobes. Here, we report a 2.0-A-resolution crystal structure of the HiLpoA N-terminal domain. Two subdomains contain tetratricopeptide-like motifs that form a concave groove, but their relative orientation differs by ~45 degrees from that observed in an NMR structure of the Escherichia coli LpoA N domain. We also determined three 2.0-2.8-A-resolution crystal structures containing four independent full-length HiLpoA molecules. In contrast to an elongated model previously suggested for E. coli LpoA, each HiLpoA formed a U-shaped structure with a different C-domain orientation. This resulted from both N-domain twisting and rotation of the C domain (up to 30 degrees ) at the end of the relatively immobile interdomain linker. Moreover, a previously predicted hinge between the lobes of the LpoA C domain exhibited variations of up to 12 degrees . Small-angle X-ray scattering (SAXS) data revealed excellent agreement with a model calculated by normal mode analysis (NMA) from one of the full-length HiLpoA molecules, but even better agreement with an ensemble of this molecule and two of the partially extended NMA-predicted models. The different LpoA structures helped explain how an outer membrane-anchored LpoA can either withdraw from or extend toward the inner membrane-bound PBP1A through peptidoglycan gaps and hence regulate the synthesis of peptidoglycan necessary for bacterial viability. | |||
Structural analyses of the Haemophilus influenzae peptidoglycan synthase activator LpoA suggest multiple conformations in solution.,Sathiyamoorthy K, Vijayalakshmi J, Tirupati B, Fan L, Saper MA J Biol Chem. 2017 Sep 8. pii: jbc.M117.804997. doi: 10.1074/jbc.M117.804997. PMID:28887305<ref>PMID:28887305</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: Saper, M | <div class="pdbe-citations 5vbg" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Saper, M A]] | |||
[[Category: Sathiyamoorthy, K]] | [[Category: Sathiyamoorthy, K]] | ||
[[Category: Biosynthetic protein]] | |||
[[Category: Gram-negative bacteria]] | |||
[[Category: Lipoprotein activator of pbp1a]] | |||
[[Category: Outer membrane lipoprotein]] | |||
[[Category: Peptidoglycan]] | |||