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1xt8
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1XT8 is a | + | 1XT8 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XT8 OCA]. |
==Reference== | ==Reference== | ||
| - | + | <ref group="xtra">PMID:15948956</ref><references group="xtra"/> | |
[[Category: Campylobacter jejuni]] | [[Category: Campylobacter jejuni]] | ||
| - | [[Category: Single protein]] | ||
[[Category: Blagova, E.]] | [[Category: Blagova, E.]] | ||
[[Category: Brannigan, J A.]] | [[Category: Brannigan, J A.]] | ||
| Line 44: | Line 43: | ||
[[Category: Structural proteomics in europe]] | [[Category: Structural proteomics in europe]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 18:24:01 2009'' |
Revision as of 16:24, 16 February 2009
Crystal Structure of Cysteine-Binding Protein from Campylobacter jejuni at 2.0 A Resolution
Template:ABSTRACT PUBMED 15948956
About this Structure
1XT8 is a 2 chains structure of sequences from Campylobacter jejuni. Full crystallographic information is available from OCA.
Reference
- Muller A, Thomas GH, Horler R, Brannigan JA, Blagova E, Levdikov VM, Fogg MJ, Wilson KS, Wilkinson AJ. An ATP-binding cassette-type cysteine transporter in Campylobacter jejuni inferred from the structure of an extracytoplasmic solute receptor protein. Mol Microbiol. 2005 Jul;57(1):143-55. PMID:15948956 doi:10.1111/j.1365-2958.2005.04691.x
Page seeded by OCA on Mon Feb 16 18:24:01 2009
Categories: Campylobacter jejuni | Blagova, E. | Brannigan, J A. | Fogg, M J. | Horler, R. | Levdikov, V M. | Muller, A. | SPINE, Structural Proteomics in Europe. | Thomas, G H. | Wilkinson, A J. | Wilson, K S. | Abc transport | Amino-acid transporter periplasmic solute-binding protein | Cysteine uptake | Spine | Structural genomic | Structural proteomics in europe
