1mdo
From Proteopedia
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|PDB= 1mdo |SIZE=350|CAPTION= <scene name='initialview01'>1mdo</scene>, resolution 1.70Å | |PDB= 1mdo |SIZE=350|CAPTION= <scene name='initialview01'>1mdo</scene>, resolution 1.70Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PMP:4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE'>PMP</scene> | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PMP:4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE'>PMP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1mdx|1MDX]], [[1mdz|1MDZ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mdo OCA], [http://www.ebi.ac.uk/pdbsum/1mdo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mdo RCSB]</span> | ||
}} | }} | ||
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[[Category: Tresser, J.]] | [[Category: Tresser, J.]] | ||
[[Category: Wright, T.]] | [[Category: Wright, T.]] | ||
| - | [[Category: PMP]] | ||
[[Category: type 1 aminotransferase fold]] | [[Category: type 1 aminotransferase fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:14:46 2008'' |
Revision as of 19:14, 30 March 2008
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| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1MDX, 1MDZ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of ArnB aminotransferase with pyridomine 5' phosphate
Overview
Lipid A modification with 4-amino-4-deoxy-L-arabinose confers on certain pathogenic bacteria, such as Salmonella, resistance to cationic antimicrobial peptides, including those derived from the innate immune system. ArnB catalysis of amino group transfer from glutamic acid to the 4"-position of a UDP-linked ketopyranose molecule to form UDP-4-amino-4-deoxy-L-arabinose represents a key step in the lipid A modification pathway. Structural and functional studies of the ArnB aminotransferase were undertaken by combining X-ray crystallography with biochemical analyses. High-resolution crystal structures were solved for two native forms and one covalently inhibited form of S. typhimurium ArnB. These structures permitted identification of key residues involved in substrate binding and catalysis, including a rarely observed nonprolyl cis peptide bond in the active site.
About this Structure
1MDO is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.
Reference
Structural studies of Salmonella typhimurium ArnB (PmrH) aminotransferase: a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme., Noland BW, Newman JM, Hendle J, Badger J, Christopher JA, Tresser J, Buchanan MD, Wright TA, Rutter ME, Sanderson WE, Muller-Dieckmann HJ, Gajiwala KS, Buchanan SG, Structure. 2002 Nov;10(11):1569-80. PMID:12429098
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