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| | <StructureSection load='6pon' size='340' side='right'caption='[[6pon]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='6pon' size='340' side='right'caption='[[6pon]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6pon]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"diplococcus_pneumoniae"_(klein_1884)_weichselbaum_1886 "diplococcus pneumoniae" (klein 1884) weichselbaum 1886]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PON FirstGlance]. <br> | + | <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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pavA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 "Diplococcus pneumoniae" (Klein 1884) Weichselbaum 1886])</td></tr> | + | </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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6pon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pon OCA], [http://pdbe.org/6pon PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pon RCSB], [http://www.ebi.ac.uk/pdbsum/6pon PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pon ProSAT]</span></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> | | </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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Manne, K]] | + | [[Category: Streptococcus pneumoniae]] |
| - | [[Category: Narayana, S V.L]] | + | [[Category: Manne K]] |
| - | [[Category: Cell adhesion]] | + | [[Category: Narayana SVL]] |
| - | [[Category: Fibronectin-binding protein]]
| + | |
| - | [[Category: Pava]]
| + | |
| - | [[Category: Pneumococcal adherence and virulence factor some]]
| + | |
| Structural highlights
Function
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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Holmes AR, McNab R, Millsap KW, Rohde M, Hammerschmidt S, Mawdsley JL, Jenkinson HF. The pavA gene of Streptococcus pneumoniae encodes a fibronectin-binding protein that is essential for virulence. Mol Microbiol. 2001 Sep;41(6):1395-408. PMID:11580843 doi:10.1046/j.1365-2958.2001.02610.x
- ↑ Manne K, Narayana SVL, Chattopadhyay D. Crystal structure of the N-terminal domain of the fibronectin-binding protein PavA from Streptococcus pneumoniae. Acta Crystallogr F Struct Biol Commun. 2019 Oct 1;75(Pt 10):657-662. doi:, 10.1107/S2053230X19012160. Epub 2019 Sep 24. PMID:31584015 doi:http://dx.doi.org/10.1107/S2053230X19012160
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