1vfl
From Proteopedia
(New page: 200px<br /><applet load="1vfl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vfl, resolution 1.80Å" /> '''Adenosine deaminase'...) |
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| - | [[Image:1vfl.gif|left|200px]]<br /><applet load="1vfl" size=" | + | [[Image:1vfl.gif|left|200px]]<br /><applet load="1vfl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vfl, resolution 1.80Å" /> | caption="1vfl, resolution 1.80Å" /> | ||
'''Adenosine deaminase'''<br /> | '''Adenosine deaminase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Structural snapshots corresponding to various states enable elucidation of | + | 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 Structure== | ==About this Structure== | ||
| - | 1VFL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1VFL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VFL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: beta-barel]] | [[Category: beta-barel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:34:45 2008'' |
Revision as of 13:34, 21 February 2008
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Adenosine deaminase
Overview
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 Structure
1VFL is a Single protein structure of sequence from Bos taurus with as ligand. Active as Adenosine deaminase, with EC number 3.5.4.4 Full crystallographic information is available from OCA.
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:16060665
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