1vfl: Difference between revisions
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[[Image:1vfl.gif|left|200px]] | [[Image:1vfl.gif|left|200px]] | ||
'''Adenosine deaminase''' | {{Structure | ||
|PDB= 1vfl |SIZE=350|CAPTION= <scene name='initialview01'>1vfl</scene>, resolution 1.80Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Adenosine_deaminase Adenosine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.4 3.5.4.4] | |||
|GENE= | |||
}} | |||
'''Adenosine deaminase''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1VFL is a [ | 1VFL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VFL OCA]. | ||
==Reference== | ==Reference== | ||
Structural basis of compound recognition by adenosine deaminase., Kinoshita T, Nakanishi I, Terasaka T, Kuno M, Seki N, Warizaya M, Matsumura H, Inoue T, Takano K, Adachi H, Mori Y, Fujii T, Biochemistry. 2005 Aug 9;44(31):10562-9. PMID:[http:// | Structural basis of compound recognition by adenosine deaminase., Kinoshita T, Nakanishi I, Terasaka T, Kuno M, Seki N, Warizaya M, Matsumura H, Inoue T, Takano K, Adachi H, Mori Y, Fujii T, Biochemistry. 2005 Aug 9;44(31):10562-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16060665 16060665] | ||
[[Category: Adenosine deaminase]] | [[Category: Adenosine deaminase]] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
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[[Category: beta-barel]] | [[Category: beta-barel]] | ||
''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 14:44:52 2008'' | ||
Revision as of 15:44, 20 March 2008
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| , resolution 1.80Å | |||||||
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| Ligands: | |||||||
| Activity: | Adenosine deaminase, with EC number 3.5.4.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Adenosine deaminase
OverviewOverview
Structural snapshots corresponding to various states enable elucidation of the molecular recognition mechanism of enzymes. Adenosine deaminase has two distinct conformations, an open form and a closed form, although it has so far been unclear what factors influence adaptation of the alternative conformations. Herein, we have determined the first nonligated structure as an initial state, which was the open form, and have thereby rationally deduced the molecular recognition mechanism. Inspection of the active site in the nonligated and ligated states indicated that occupancy at one of the water-binding positions in the nonligated state was highly significant in determining alternate conformations. When this position is empty, subsequent movement of Phe65 toward the space induces the closed form. On the other hand, while occupied, the overall conformation remains in the open form. This structural understanding should greatly assist structure-oriented drug design and enable control of the enzymatic activity.
About this StructureAbout this Structure
1VFL is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of compound recognition by adenosine deaminase., Kinoshita T, Nakanishi I, Terasaka T, Kuno M, Seki N, Warizaya M, Matsumura H, Inoue T, Takano K, Adachi H, Mori Y, Fujii T, Biochemistry. 2005 Aug 9;44(31):10562-9. PMID:16060665
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