4naz: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
{{STRUCTURE_4naz| PDB=4naz | SCENE= }} | |||
===Crystal Structure of FosB from Staphylococcus aureus with Zn and Sulfate at 1.15 Angstrom Resolution=== | |||
{{ABSTRACT_PUBMED_24447055}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/FOSB_STAAN FOSB_STAAN]] Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor (By similarity). | |||
==About this Structure== | |||
[[4naz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NAZ OCA]. | |||
==Reference== | |||
<ref group="xtra">PMID:024447055</ref><references group="xtra"/><references/> | |||
[[Category: Cook, P D.]] | |||
[[Category: Goodman, M C.]] | |||
[[Category: Harp, J.]] | |||
[[Category: Jagessar, K.]] | |||
[[Category: Keithly, M E.]] | |||
[[Category: Bacillithiol-s-transferase]] | |||
[[Category: Transferase]] | |||
Revision as of 20:55, 3 March 2014
Crystal Structure of FosB from Staphylococcus aureus with Zn and Sulfate at 1.15 Angstrom ResolutionCrystal Structure of FosB from Staphylococcus aureus with Zn and Sulfate at 1.15 Angstrom Resolution
Template:ABSTRACT PUBMED 24447055
FunctionFunction
[FOSB_STAAN] Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor (By similarity).
About this StructureAbout this Structure
4naz is a 1 chain structure. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Thompson MK, Keithly ME, Goodman MC, Hammer ND, Cook PD, Jagessar KL, Harp J, Skaar EP, Armstrong RN. Structure and Function of the Genomically Encoded Fosfomycin Resistance Enzyme, FosB, from Staphylococcus aureus. Biochemistry. 2014 Feb 4;53(4):755-65. doi: 10.1021/bi4015852. Epub 2014 Jan 21. PMID:24447055 doi:http://dx.doi.org/10.1021/bi4015852