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6pon
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF FIBRONECTIN- BINDING PROTEIN PAVA FROM STREPTOCOCCUS PNEUMONIAE== | |
| + | <StructureSection load='6pon' size='340' side='right'caption='[[6pon]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6pon]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PON FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.395Å</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=6pon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pon OCA], [https://pdbe.org/6pon PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pon RCSB], [https://www.ebi.ac.uk/pdbsum/6pon PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pon ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RQCH_STRR6 RQCH_STRR6] Part of the ribosome quality control system (RQC). Recruits Ala-charged tRNA and directs the elongation of stalled nascent chains on 50S ribosomal subunits, leading to non-templated C-terminal Ala extensions (Ala tail). The Ala tail promotes nascent chain degradation. May add between 1 and at least 8 Ala residues. Binds to stalled 50S ribosomal subunits.[HAMAP-Rule:MF_00844] Recombinant protein binds to immobilized human fibronectin; binding is saturable and competed by heparin. Recombinant protein inhibits binding of whole cells to fibronectin.<ref>PMID:11580843</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The Gram-positive bacterium Streptococcus pneumoniae, a major human pathogen, is a regular colonizer of the upper and lower respiratory tracts. Pneumococcal adherence and virulence factor A (PavA), a fibronectin-binding bacterial protein, from S. pneumoniae is an important facilitator of its colonization of host cells. In this study, the crystal structure of the N-terminal domain of PavA (SpPavA-N) determined at a resolution of 2.39 A is reported. Each monomer of the dimeric protein consists of two domains (domains I and II) and a short alpha-helix (alpha6) at the C-terminus that are connected by elongated loops. Comparison of the SpPavA-N structure with that of its homolog from Streptococcus suis (FBPS-N) revealed differences in alpha5, alpha6 and the domain II/alpha6 inter-loop region within domain II. The alpha5 helix of FBPS-N folds back toward domain I, whereas in SpPavA-N it adopts an elongated rod shape. | ||
| - | + | Crystal structure of the N-terminal domain of the fibronectin-binding protein PavA from Streptococcus pneumoniae.,Manne K, Narayana SVL, Chattopadhyay D Acta Crystallogr F Struct Biol Commun. 2019 Oct 1;75(Pt 10):657-662. doi:, 10.1107/S2053230X19012160. Epub 2019 Sep 24. PMID:31584015<ref>PMID:31584015</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6pon" style="background-color:#fffaf0;"></div> |
| - | [[Category: Manne | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptococcus pneumoniae]] | ||
| + | [[Category: Manne K]] | ||
| + | [[Category: Narayana SVL]] | ||
Current revision
CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF FIBRONECTIN- BINDING PROTEIN PAVA FROM STREPTOCOCCUS PNEUMONIAE
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