Bis-methionyl coordination in the crystal structure of the heme-binding domain of the streptococcal cell surface protein Shp

Surface proteins Shr, Shp, and the ATP-binding cassette (ABC) transporter HtsABC are believed to make up the machinery for heme uptake in Streptococcus pyogenes. Shp transfers its heme to HtsA, the lipoprotein component of HtsABC, providing the only experimentally demonstrated example of direct heme...

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Bibliographic Details
Main Authors:	Aranda, Roman, Worley, Chad E., Liu, Mengyao, Bitto, Eduard, Cates, M. Susan, Olson, John S., Lei, Benfang, Phillips, George N.
Format:	Artigo
Language:	Inglês
Published:	2007
Subjects:	Article
Online Access:	https://ncbi.nlm.nih.gov/pmc/articles/PMC2386982/ https://ncbi.nlm.nih.gov/pubmed/17920629 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2007.08.058
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Bis-methionyl coordination in the crystal structure of the heme-binding domain of the streptococcal cell surface protein Shp

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