1hsk
From Proteopedia
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|PDB= 1hsk |SIZE=350|CAPTION= <scene name='initialview01'>1hsk</scene>, resolution 2.30Å | |PDB= 1hsk |SIZE=350|CAPTION= <scene name='initialview01'>1hsk</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/UDP-N-acetylmuramate_dehydrogenase UDP-N-acetylmuramate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.158 1.1.1.158] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-N-acetylmuramate_dehydrogenase UDP-N-acetylmuramate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.158 1.1.1.158] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hsk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hsk OCA], [http://www.ebi.ac.uk/pdbsum/1hsk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hsk RCSB]</span> | ||
}} | }} | ||
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[[Category: Herberg, J T.]] | [[Category: Herberg, J T.]] | ||
[[Category: Jr., J P.Martin.]] | [[Category: Jr., J P.Martin.]] | ||
| - | [[Category: FAD]] | ||
[[Category: cell division]] | [[Category: cell division]] | ||
[[Category: cell wall]] | [[Category: cell wall]] | ||
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[[Category: peptidoglycan synthesis]] | [[Category: peptidoglycan synthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:09:54 2008'' |
Revision as of 18:09, 30 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | UDP-N-acetylmuramate dehydrogenase, with EC number 1.1.1.158 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF S. AUREUS MURB
Overview
The X-ray crystal structure of the substrate free form of Staphylococcus aureus UDP-N-acetylenolpyruvylglucosamine reductase (MurB) has been solved to 2.3 A resolution with an R-factor of 20.3% and a free R-factor of 22.3%. While the overall fold of the S. aureus enzyme is similar to that of the homologous Escherichia coli MurB X-ray crystal structure, notable distinctions between the S. aureus and E. coli MurB protein structures occur in residues involved in substrate binding. Analysis of available MurB sequences from other bacteria suggest that the S. aureus MurB structure is representative of a distinct structural class of UDP-N-acetylenolpyruvylglucosamine reductases including Bacillus subtilis and Helicobacter pylori that are characterized by a modified mechanism for substrate binding.
About this Structure
1HSK is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
A structural variation for MurB: X-ray crystal structure of Staphylococcus aureus UDP-N-acetylenolpyruvylglucosamine reductase (MurB)., Benson TE, Harris MS, Choi GH, Cialdella JI, Herberg JT, Martin JP Jr, Baldwin ET, Biochemistry. 2001 Feb 27;40(8):2340-50. PMID:11327854
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