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  Solution structure of the histidine-containing phosphocarrier protein from Staphylococcus carnosus

Görler, A., Hengstenberg, W., Kravanja, M., Beneicke, W., Maurer, T., & Kalbitzer, H. R. (1999). Solution structure of the histidine-containing phosphocarrier protein from Staphylococcus carnosus. Applied Magnetic Resonance, 17(2), 465-480. Retrieved from http://link.springer.com/article/10.1007/BF03162178.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-57FD-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-57FE-7
Genre: Journal Article
Alternative Title : Solution structure of the histidine-containing phosphocarrier protein from Staphylococcus carnosus

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 Creators:
Görler, Adrian1, Author              
Hengstenberg, Wolfgang, Author
Kravanja, M., Author
Beneicke, Wolfgang1, Author              
Maurer, Till2, Author              
Kalbitzer, Hans Robert1, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              

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 Abstract: The solution structure of histidine-containing phosphocarrier protein from Staphylococcus carnosus was determined by two- and three-dimensional nuclear magnetic resonance (NMR) spectroscopy on uniformly 15N-enriched protein. The main structural element is an antiparallel beta-pleated sheet with four strands A, B, C, and D arranged with the topology A-D-B-C. Strand A comprises residues 2 to 8, strand B residues 32 to 37, strand C reidues 40 to 43, and strand D residues 59 to 66. Three right-handed helices are arranged on top of the beta-pleated sheet. Helix a reaches from residue 16 to 29, helix b from residue 48 to 53, and helix c from residue 72 to 83. Strands B and C of the beta-pleated sheet are connected by a type II turn. The hydroxyl proton of Ser-31 is ex-changing with the solvent so slowly that cross peaks can be detected in two-dimensional NMR spectra based on homonuclear J-couplings. The imidazole ring of the active-center His-15, which is partly charged in the structure determined at pH 7.2, is located above the N-terminal end of helix a, perpendicular to its axis. The Nδ1 atom of His-15, accepting the phosphoryl from enzyme I, is exposed to the solvent

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Language(s): eng - English
 Dates: 1999-08-281999-06-011999
 Publication Status: Published in print
 Pages: 16
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 666535
URI: http://link.springer.com/article/10.1007/BF03162178
Other: 4418
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Title: Applied Magnetic Resonance
Source Genre: Journal
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Publ. Info: Springer-Verlag
Pages: - Volume / Issue: 17 (2) Sequence Number: - Start / End Page: 465 - 480 Identifier: ISSN: 0937-9347
CoNE: https://pure.mpg.de/cone/journals/resource/0937-9347