1wxy
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(New page: 200px<br /><applet load="1wxy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wxy, resolution 2.50Å" /> '''Crystal structure of...)
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Revision as of 03:37, 21 November 2007
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Crystal structure of adenosine deaminase ligated with a potent inhibitor
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
1WXY is a Single protein structure of sequence from Bos taurus with ZN and FRK as ligands. 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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