2cdn: Difference between revisions

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==Overview==

The crystal structure of Mycobacterium tuberculosis adenylate kinase, (MtAK) in complex with two ADP molecules and Mg2+ has been determined at, 1.9 A resolution. Comparison with the solution structure of the enzyme, obtained in the absence of substrates, shows significant conformational, changes of the LID and NMP-binding domains upon substrate binding. The, ternary complex represents the state of the enzyme at the start of the, backward reaction (ATP synthesis). The structure is consistent with a, direct nucleophilic attack of a terminal oxygen from the acceptor ADP, molecule on the beta-phosphate from the donor substrate, and both the, geometry and the distribution of positive charge in the active site, support the hypothesis of an associative mechanism for phosphoryl, transfer.

The crystal structure of Mycobacterium tuberculosis adenylate kinase (MtAK) in complex with two ADP molecules and Mg2+ has been determined at 1.9 A resolution. Comparison with the solution structure of the enzyme, obtained in the absence of substrates, shows significant conformational changes of the LID and NMP-binding domains upon substrate binding. The ternary complex represents the state of the enzyme at the start of the backward reaction (ATP synthesis). The structure is consistent with a direct nucleophilic attack of a terminal oxygen from the acceptor ADP molecule on the beta-phosphate from the donor substrate, and both the geometry and the distribution of positive charge in the active site support the hypothesis of an associative mechanism for phosphoryl transfer.

==About this Structure==

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[[Category: Mycobacterium tuberculosis]]

[[Category: Single protein]]

[[Category: Alzari, P.M.]]

[[Category: Alzari, P M.]]

[[Category: Bellinzoni, M.]]

[[Category: Grana, M.]]

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[[Category: transferase]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:47:35 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The crystal structure of Mycobacterium tuberculosis adenylate kinase, (MtAK) in complex with two ADP molecules and Mg2+ has been determined at, 1.9 A resolution. Comparison with the solution structure of the enzyme, obtained in the absence of substrates, shows significant conformational, changes of the LID and NMP-binding domains upon substrate binding. The, ternary complex represents the state of the enzyme at the start of the, backward reaction (ATP synthesis). The structure is consistent with a, direct nucleophilic attack of a terminal oxygen from the acceptor ADP, molecule on the beta-phosphate from the donor substrate, and both the, geometry and the distribution of positive charge in the active site, support the hypothesis of an associative mechanism for phosphoryl, transfer.
+The crystal structure of Mycobacterium tuberculosis adenylate kinase (MtAK) in complex with two ADP molecules and Mg2+ has been determined at 1.9 A resolution. Comparison with the solution structure of the enzyme, obtained in the absence of substrates, shows significant conformational changes of the LID and NMP-binding domains upon substrate binding. The ternary complex represents the state of the enzyme at the start of the backward reaction (ATP synthesis). The structure is consistent with a direct nucleophilic attack of a terminal oxygen from the acceptor ADP molecule on the beta-phosphate from the donor substrate, and both the geometry and the distribution of positive charge in the active site support the hypothesis of an associative mechanism for phosphoryl transfer.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Mycobacterium tuberculosis]]
 [[Category: Single protein]]
-[[Category: Alzari, P.M.]]
+[[Category: Alzari, P M.]]
 [[Category: Bellinzoni, M.]]
 [[Category: Grana, M.]]
@@ Line 30: / Line 30: @@
 [[Category: transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:34:11 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:47:35 2008''