4p29
From Proteopedia
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<StructureSection load='4p29' size='340' side='right'caption='[[4p29]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='4p29' size='340' side='right'caption='[[4p29]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4p29]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P29 OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[4p29]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae_Rd_KW20 Haemophilus influenzae Rd KW20]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P29 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9500648Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4p29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p29 OCA], [https://pdbe.org/4p29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p29 RCSB], [https://www.ebi.ac.uk/pdbsum/4p29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p29 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == 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> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Haemophilus influenzae Rd KW20]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Saper | + | [[Category: Saper MA]] |
| - | [[Category: Vijayalakshmi | + | [[Category: Vijayalakshmi J]] |
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Current revision
Crystal structure of the LpoA N-terminal domain from Haemophilus influenzae
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