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6pon

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CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF FIBRONECTIN- BINDING PROTEIN PAVA FROM STREPTOCOCCUS PNEUMONIAE

Structural highlights

6pon is a 2 chain structure with sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.395Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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