1mfz

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(New page: 200px<br /><applet load="1mfz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mfz, resolution 2.8&Aring;" /> '''Partially refined 2.8...)
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[[Image:1mfz.gif|left|200px]]<br /><applet load="1mfz" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1mfz.gif|left|200px]]<br /><applet load="1mfz" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1mfz, resolution 2.8&Aring;" />
caption="1mfz, resolution 2.8&Aring;" />
'''Partially refined 2.8 A Crystal structure of GDP-mannose dehydrogenase from P. aeruginosa'''<br />
'''Partially refined 2.8 A Crystal structure of GDP-mannose dehydrogenase from P. aeruginosa'''<br />
==Overview==
==Overview==
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The enzyme GMD from Pseudomonas aeruginosa catalyzes the committed step in, the synthesis of the exopolysaccharide alginate. Alginate is a major, component of P. aeruginosa biofilms that protect the bacteria from the, host immune response and antibiotic therapy. The 1.55 A crystal structure, of GMD in ternary complex with its cofactor NAD(H) and product, GDP-mannuronic acid reveals that the enzyme forms a domain-swapped dimer, with two polypeptide chains contributing to each active site. The, extensive dimer interface provides multiple opportunities for intersubunit, communication. Comparison of the GMD structure with that of UDP-glucose, dehydrogenase reveals the structural basis of sugar binding specificity, that distinguishes these two related enzyme families. The high-resolution, structure of GMD provides detailed information on the active site of the, enzyme and a template for structure-based inhibitor design.
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The enzyme GMD from Pseudomonas aeruginosa catalyzes the committed step in the synthesis of the exopolysaccharide alginate. Alginate is a major component of P. aeruginosa biofilms that protect the bacteria from the host immune response and antibiotic therapy. The 1.55 A crystal structure of GMD in ternary complex with its cofactor NAD(H) and product GDP-mannuronic acid reveals that the enzyme forms a domain-swapped dimer with two polypeptide chains contributing to each active site. The extensive dimer interface provides multiple opportunities for intersubunit communication. Comparison of the GMD structure with that of UDP-glucose dehydrogenase reveals the structural basis of sugar binding specificity that distinguishes these two related enzyme families. The high-resolution structure of GMD provides detailed information on the active site of the enzyme and a template for structure-based inhibitor design.
==About this Structure==
==About this Structure==
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1MFZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with GDX as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/GDP-mannose_6-dehydrogenase GDP-mannose 6-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.132 1.1.1.132] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MFZ OCA].
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1MFZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=GDX:'>GDX</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/GDP-mannose_6-dehydrogenase GDP-mannose 6-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.132 1.1.1.132] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MFZ OCA].
==Reference==
==Reference==
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[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Beamer, L.J.]]
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[[Category: Beamer, L J.]]
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[[Category: Snook, C.F.]]
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[[Category: Snook, C F.]]
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[[Category: Tipton, P.A.]]
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[[Category: Tipton, P A.]]
[[Category: GDX]]
[[Category: GDX]]
[[Category: domain-swapped dimer]]
[[Category: domain-swapped dimer]]
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[[Category: rossman fold]]
[[Category: rossman fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:23:24 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:52 2008''

Revision as of 11:54, 21 February 2008


1mfz, resolution 2.8Å

Drag the structure with the mouse to rotate

Partially refined 2.8 A Crystal structure of GDP-mannose dehydrogenase from P. aeruginosa

Overview

The enzyme GMD from Pseudomonas aeruginosa catalyzes the committed step in the synthesis of the exopolysaccharide alginate. Alginate is a major component of P. aeruginosa biofilms that protect the bacteria from the host immune response and antibiotic therapy. The 1.55 A crystal structure of GMD in ternary complex with its cofactor NAD(H) and product GDP-mannuronic acid reveals that the enzyme forms a domain-swapped dimer with two polypeptide chains contributing to each active site. The extensive dimer interface provides multiple opportunities for intersubunit communication. Comparison of the GMD structure with that of UDP-glucose dehydrogenase reveals the structural basis of sugar binding specificity that distinguishes these two related enzyme families. The high-resolution structure of GMD provides detailed information on the active site of the enzyme and a template for structure-based inhibitor design.

About this Structure

1MFZ is a Single protein structure of sequence from Pseudomonas aeruginosa with as ligand. Active as GDP-mannose 6-dehydrogenase, with EC number 1.1.1.132 Full crystallographic information is available from OCA.

Reference

Crystal structure of GDP-mannose dehydrogenase: a key enzyme of alginate biosynthesis in P. aeruginosa., Snook CF, Tipton PA, Beamer LJ, Biochemistry. 2003 Apr 29;42(16):4658-68. PMID:12705829

Page seeded by OCA on Thu Feb 21 13:54:52 2008

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