1mfz
From Proteopedia
(New page: 200px<br /><applet load="1mfz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mfz, resolution 2.8Å" /> '''Partially refined 2.8...) |
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| - | [[Image:1mfz.gif|left|200px]]<br /><applet load="1mfz" size=" | + | [[Image:1mfz.gif|left|200px]]<br /><applet load="1mfz" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mfz, resolution 2.8Å" /> | caption="1mfz, resolution 2.8Å" /> | ||
'''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== | ||
| - | The enzyme GMD from Pseudomonas aeruginosa catalyzes the committed step in | + | 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== | ||
| - | 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:// | + | 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]] | ||
| - | [[Category: Beamer, L | + | [[Category: Beamer, L J.]] |
| - | [[Category: Snook, C | + | [[Category: Snook, C F.]] |
| - | [[Category: Tipton, P | + | [[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]] | ||
| - | ''Page seeded by [http:// | + | ''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
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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
