1mdx

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(New page: 200px<br /><applet load="1mdx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mdx, resolution 1.96&Aring;" /> '''Crystal structure of...)
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[[Image:1mdx.gif|left|200px]]<br /><applet load="1mdx" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1mdx.gif|left|200px]]<br /><applet load="1mdx" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1mdx, resolution 1.96&Aring;" />
caption="1mdx, resolution 1.96&Aring;" />
'''Crystal structure of ArnB transferase with pyridoxal 5' phosphate'''<br />
'''Crystal structure of ArnB transferase with pyridoxal 5' phosphate'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1MDX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with PLP, AKG and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MDX OCA].
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1MDX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=PLP:'>PLP</scene>, <scene name='pdbligand=AKG:'>AKG</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MDX OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Badger, J.]]
[[Category: Badger, J.]]
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[[Category: Buchanan, M.D.]]
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[[Category: Buchanan, M D.]]
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[[Category: Buchanan, S.G.]]
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[[Category: Buchanan, S G.]]
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[[Category: Christopher, J.A.]]
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[[Category: Christopher, J A.]]
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[[Category: Gajiwala, K.S.]]
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[[Category: Gajiwala, K S.]]
[[Category: Hendle, J.]]
[[Category: Hendle, J.]]
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[[Category: Muller-Dieckmann, H.J.]]
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[[Category: Muller-Dieckmann, H J.]]
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[[Category: Newman, J.M.]]
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[[Category: Newman, J M.]]
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[[Category: Noland, B.W.]]
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[[Category: Noland, B W.]]
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[[Category: Rutter, M.E.]]
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[[Category: Rutter, M E.]]
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[[Category: Sanderson, W.E.]]
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[[Category: Sanderson, W E.]]
[[Category: Tresser, J.]]
[[Category: Tresser, J.]]
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[[Category: Wright, T.A.]]
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[[Category: Wright, T A.]]
[[Category: AKG]]
[[Category: AKG]]
[[Category: GOL]]
[[Category: GOL]]
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[[Category: type 1 aminotransferase fold]]
[[Category: type 1 aminotransferase fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:21:16 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:15 2008''

Revision as of 11:54, 21 February 2008


1mdx, resolution 1.96Å

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Crystal structure of ArnB transferase with pyridoxal 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

1MDX is a Single protein structure of sequence from Salmonella typhimurium with , and as ligands. 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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