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'''Unreleased structure'''


The entry 5vat is ON HOLD
==Haemophilus influenzae LpoA: Monoclinic form (Mon2) with 2 molecules per a.u.==
<StructureSection load='5vat' size='340' side='right' caption='[[5vat]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5vat]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VAT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VAT FirstGlance]. <br>
</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]], [[4p29|4p29]], [[3ckm|3ckm]], [[5vbg|5vbg]]</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=5vat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vat OCA], [http://pdbe.org/5vat PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vat RCSB], [http://www.ebi.ac.uk/pdbsum/5vat PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vat 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.


Authors: Saper, M.A., Sathiyamoorthy, K.
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>


Description: Haemophilus influenzae LpoA: Monoclinic form (Mon2) with 2 molecules per a.u.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Saper, M.A]]
<div class="pdbe-citations 5vat" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Saper, M A]]
[[Category: Sathiyamoorthy, K]]
[[Category: Sathiyamoorthy, K]]
[[Category: Binding protein]]
[[Category: Biosynthetic protein]]
[[Category: Conformational flexibility]]
[[Category: Lipoprotein]]
[[Category: Pbp1a]]
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