1u9j: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1u9j.gif|left|200px]]
{{Seed}}
[[Image:1u9j.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1u9j|  PDB=1u9j  |  SCENE=  }}  
{{STRUCTURE_1u9j|  PDB=1u9j  |  SCENE=  }}  


'''Crystal Structure of E. coli ArnA (PmrI) Decarboxylase Domain'''
===Crystal Structure of E. coli ArnA (PmrI) Decarboxylase Domain===




==Overview==
<!--
Gram-negative bacteria including Escherichia coli, Salmonella typhimurium, and Pseudomonas aeruginosa can modify the structure of lipid A in their outer membrane with 4-amino-4-deoxy-l-arabinose (Ara4N). Such modification results in resistance to cationic antimicrobial peptides of the innate immune system and antibiotics such as polymyxin. ArnA is a key enzyme in the lipid A modification pathway, and its deletion abolishes both the Ara4N-lipid A modification and polymyxin resistance. ArnA is a bifunctional enzyme. It can catalyze (i) the NAD(+)-dependent decarboxylation of UDP-glucuronic acid to UDP-4-keto-arabinose and (ii) the N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-l-arabinose. We show that the NAD(+)-dependent decarboxylating activity is contained in the 360 amino acid C-terminal domain of ArnA. This domain is separable from the N-terminal fragment, and its activity is identical to that of the full-length enzyme. The crystal structure of the ArnA decarboxylase domain from E. coli is presented here. The structure confirms that the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) family. On the basis of sequence and structure comparisons of the ArnA decarboxylase domain with other members of the short-chain dehydrogenase/reductase (SDR) family, we propose a binding model for NAD(+) and UDP-glucuronic acid and the involvement of residues T(432), Y(463), K(467), R(619), and S(433) in the mechanism of NAD(+)-dependent oxidation of the 4''-OH of the UDP-glucuronic acid and decarboxylation of the UDP-4-keto-glucuronic acid intermediate.
The line below this paragraph, {{ABSTRACT_PUBMED_15491143}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15491143 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15491143}}


==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: E coli proteome]]
[[Category: E coli proteome]]
[[Category: X-ray structure]]
[[Category: X-ray structure]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:56:08 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:32:50 2008''

Revision as of 20:32, 28 July 2008

File:1u9j.png

Template:STRUCTURE 1u9j

Crystal Structure of E. coli ArnA (PmrI) Decarboxylase Domain

Template:ABSTRACT PUBMED 15491143

About this Structure

1U9J is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of Escherichia coli ArnA (PmrI) decarboxylase domain. A key enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance., Gatzeva-Topalova PZ, May AP, Sousa MC, Biochemistry. 2004 Oct 26;43(42):13370-9. PMID:15491143

Page seeded by OCA on Mon Jul 28 23:32:50 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1u9j&oldid=718808"