1z7e

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[[Image:1z7e.gif|left|200px]]<br /><applet load="1z7e" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1z7e.gif|left|200px]]
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caption="1z7e, resolution 3.00&Aring;" />
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'''Crystal structure of full length ArnA'''<br />
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{{Structure
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|PDB= 1z7e |SIZE=350|CAPTION= <scene name='initialview01'>1z7e</scene>, resolution 3.00&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> and <scene name='pdbligand=UGA:URIDINE-5'-DIPHOSPHATE-GLUCURONIC ACID'>UGA</scene>
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|ACTIVITY=
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|GENE= PMRI, YFBG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''Crystal structure of full length ArnA'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1Z7E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=UGA:'>UGA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z7E OCA].
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1Z7E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z7E OCA].
==Reference==
==Reference==
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Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance., Gatzeva-Topalova PZ, May AP, Sousa MC, Structure. 2005 Jun;13(6):929-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15939024 15939024]
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Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance., Gatzeva-Topalova PZ, May AP, Sousa MC, Structure. 2005 Jun;13(6):929-42. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15939024 15939024]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: rossmann fold; ob-like fold]]
[[Category: rossmann fold; ob-like fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:32:03 2008''

Revision as of 13:32, 20 March 2008


PDB ID 1z7e

Drag the structure with the mouse to rotate
, resolution 3.00Å
Ligands: and
Gene: PMRI, YFBG (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



Crystal structure of full length ArnA


Overview

The modification of lipid A with 4-amino-4-deoxy-L-arabinose (Ara4N) allows gram-negative bacteria to resist the antimicrobial activity of cationic antimicrobial peptides and antibiotics such as polymyxin. ArnA is the first enzyme specific to the lipid A-Ara4N pathway. It contains two functionally and physically separable domains: a dehydrogenase domain (ArnA_DH) catalyzing the NAD+-dependent oxidative decarboxylation of UDP-Glucuronic acid (UDP-GlcA), and a transformylase domain that formylates UDP-Ara4N. Here, we describe the crystal structure of the full-length bifunctional ArnA with UDP-GlcA and ATP bound to the dehydrogenase domain. Binding of UDP-GlcA triggers a 17 A conformational change in ArnA_DH that opens the NAD+ binding site while trapping UDP-GlcA. We propose an ordered mechanism of substrate binding and product release. Mutation of residues R619 and S433 demonstrates their importance in catalysis and suggests that R619 functions as a general acid in catalysis. The proposed mechanism for ArnA_DH has important implications for the design of selective inhibitors.

About this Structure

1Z7E is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance., Gatzeva-Topalova PZ, May AP, Sousa MC, Structure. 2005 Jun;13(6):929-42. PMID:15939024

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