1mdo: Difference between revisions

Revision as of 23:44, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1mdo.png

Template:STRUCTURE 1mdo

Crystal structure of ArnB aminotransferase with pyridomine 5' phosphateCrystal structure of ArnB aminotransferase with pyridomine 5' phosphate

Template:ABSTRACT PUBMED 12429098

About this StructureAbout this Structure

1MDO is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Wed Jul 2 23:44:41 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of ArnB aminotransferase with pyridomine 5' phosphate'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12429098}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12429098 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12429098}}
 ==About this Structure==
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 [[Category: Wright, T.]]
 [[Category: Type 1 aminotransferase fold]]
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