A Helical String of Alternately Connected Three-Helix Bundles for the Cell Wall-Associated Adhesion Protein Ebh from Staphylococcus aureus
Structure, ISSN: 0969-2126, Vol: 16, Issue: 3, Page: 488-496
2008
- 24Citations
- 40Captures
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Metrics Details
- Citations24
- Citation Indexes24
- CrossRef24
- 24
- Captures40
- Readers40
- 40
Article Description
The 1.1 MDa cell-wall-associated adhesion protein of staphylococci, Ebh, consists of several distinct regions, including a large central region with 52 imperfect repeats of 126 amino acid residues. We investigated the structure of this giant molecule by X-ray crystallography, circular dichroism (CD) spectrometry, and small-angle X-ray scattering (SAXS). The crystal structure of two repeats showed that each repeat consists of two distinct three-helix bundles, and two such repeats are connected along the long axis, resulting in a rod-like structure that is 120 Å in length. CD and SAXS analyses of the samples with longer repeats suggested that each repeat has an identical structure, and that such repeats are connected tandemly to form a rod-like structure in solution, the length of which increased proportionately with the number of repeating units. On the basis of these results, it was proposed that Ebh is a 320 nm rod-like molecule with some plasticity at module junctions.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0969212608000245; http://dx.doi.org/10.1016/j.str.2007.12.018; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=40049083075&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/18334223; https://linkinghub.elsevier.com/retrieve/pii/S0969212608000245; http://www.cell.com/structure/abstract/S0969-2126(08)00024-5?_returnURL=http%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS0969212608000245%3Fshowall%3Dtrue; http://linkinghub.elsevier.com/retrieve/pii/S0969212608000245; https://secure.jbs.elsevierhealth.com/action/getSharedSiteSession?redirect=http%3A%2F%2Fwww.cell.com%2Fstructure%2Fabstract%2FS0969-2126%2808%2900024-5%3F_returnURL%3Dhttp%253A%252F%252Flinkinghub.elsevier.com%252Fretrieve%252Fpii%252FS0969212608000245%253Fshowall%253Dtrue&rc=0&code=cell-site; http://acw.elsevier.com/SSOCore?return=https%3A%2F%2Fsecure.jbs.elsevierhealth.com%2Faction%2FconsumeSsoCookie%3FredirectUri%3Dhttp%253A%252F%252Fwww.cell.com%252Faction%252FconsumeSharedSessionAction%253FJSESSIONID%253DaaawzGuVMot7QbB5C33xv%2526MAID%253DodcLKJWP355D9doWM4MieA%25253D%25253D%2526SERVER%253DWZ6myaEXBLEIcey8uceZQQ%25253D%25253D%2526ORIGIN%253D969653561%2526RD%253DRD; http://acw.elsevier.com/SSOCore/?return=https%3A%2F%2Fsecure.jbs.elsevierhealth.com%2Faction%2FconsumeSsoCookie%3FredirectUri%3Dhttp%253A%252F%252Fwww.cell.com%252Faction%252FconsumeSharedSessionAction%253FJSESSIONID%253DaaawzGuVMot7QbB5C33xv%2526MAID%253DodcLKJWP355D9doWM4MieA%25253D%25253D%2526SERVER%253DWZ6myaEXBLEIcey8uceZQQ%25253D%25253D%2526ORIGIN%253D969653561%2526RD%253DRD; https://secure.jbs.elsevierhealth.com/action/consumeSsoCookie?redirectUri=http%3A%2F%2Fwww.cell.com%2Faction%2FconsumeSharedSessionAction%3FJSESSIONID%3DaaawzGuVMot7QbB5C33xv%26MAID%3DodcLKJWP355D9doWM4MieA%253D%253D%26SERVER%3DWZ6myaEXBLEIcey8uceZQQ%253D%253D%26ORIGIN%3D969653561%26RD%3DRD&acw=&utt=
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