1e9y
From Proteopedia
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| - | [[Image:1e9y.gif|left|200px]] | + | [[Image:1e9y.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF HELICOBACTER PYLORI UREASE IN COMPLEX WITH ACETOHYDROXAMIC ACID''' | + | {{Structure |
| + | |PDB= 1e9y |SIZE=350|CAPTION= <scene name='initialview01'>1e9y</scene>, resolution 3.0Å | ||
| + | |SITE= <scene name='pdbsite=NI1:Ni+Binding+Site+For+Residue+B2002'>NI1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene> and <scene name='pdbligand=HAE:ACETOHYDROXAMIC ACID'>HAE</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF HELICOBACTER PYLORI UREASE IN COMPLEX WITH ACETOHYDROXAMIC ACID''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1E9Y is a [ | + | 1E9Y is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E9Y OCA]. |
==Reference== | ==Reference== | ||
| - | Supramolecular assembly and acid resistance of Helicobacter pylori urease., Ha NC, Oh ST, Sung JY, Cha KA, Lee MH, Oh BH, Nat Struct Biol. 2001 Jun;8(6):505-9. PMID:[http:// | + | Supramolecular assembly and acid resistance of Helicobacter pylori urease., Ha NC, Oh ST, Sung JY, Cha KA, Lee MH, Oh BH, Nat Struct Biol. 2001 Jun;8(6):505-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11373617 11373617] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Ha, N C.]] | [[Category: Ha, N C.]] | ||
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[[Category: urease]] | [[Category: urease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:52:24 2008'' |
Revision as of 08:52, 20 March 2008
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| , resolution 3.0Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HELICOBACTER PYLORI UREASE IN COMPLEX WITH ACETOHYDROXAMIC ACID
Overview
Helicobacter pylori, an etiologic agent in a variety of gastroduodenal diseases, produces a large amount of urease, which is believed to neutralize gastric acid by producing ammonia for the survival of the bacteria. Up to 30% of the enzyme associates with the surface of intact cells upon lysis of neighboring bacteria. The role of the enzyme at the extracellular location has been a subject of controversy because the purified enzyme is irreversibly inactivated below pH 5. We have determined the crystal structure of H. pylori urease, which has a 1.1 MDa spherical assembly of 12 catalytic units with an outer diameter of approximately 160 A. Under physiologically relevant conditions, the activity of the enzyme remains unaffected down to pH 3. Activity assays under different conditions indicated that the cluster of the 12 active sites on the supramolecular assembly may be critical for the survival of the enzyme at low pH. The structure provides a novel example of a molecular assembly adapted for acid resistance that, together with the low Km value of the enzyme, is likely to enable the organism to inhabit the hostile niche.
About this Structure
1E9Y is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Supramolecular assembly and acid resistance of Helicobacter pylori urease., Ha NC, Oh ST, Sung JY, Cha KA, Lee MH, Oh BH, Nat Struct Biol. 2001 Jun;8(6):505-9. PMID:11373617
Page seeded by OCA on Thu Mar 20 10:52:24 2008
Categories: Protein complex | Ha, N C. | Oh, B H. | Oh, S T. | HAE | NI | Acetohydroxamic acid | Dodecamer | Helicobacter | Hydrolase | Urease
