1ckm: Difference between revisions

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==Overview==

We have solved the crystal structure of an mRNA capping enzyme at 2.5 A, resolution. The enzyme comprises two domains with a deep, but narrow, cleft between them. The two molecules in the crystallographic asymmetric, unit adopt very different conformations; both contain a bound GTP, but one, protein molecule is in an open conformation while the other is in a closed, conformation. Only in the closed conformation is the enzyme able to bind, manganese ions and undergo catalysis within the crystals to yield the, covalent guanylated enzyme intermediate. These structures provide direct, evidence for a mechanism that involves a significant conformational change, in the enzyme during catalysis.

We have solved the crystal structure of an mRNA capping enzyme at 2.5 A resolution. The enzyme comprises two domains with a deep, but narrow, cleft between them. The two molecules in the crystallographic asymmetric unit adopt very different conformations; both contain a bound GTP, but one protein molecule is in an open conformation while the other is in a closed conformation. Only in the closed conformation is the enzyme able to bind manganese ions and undergo catalysis within the crystals to yield the covalent guanylated enzyme intermediate. These structures provide direct evidence for a mechanism that involves a significant conformational change in the enzyme during catalysis.

==About this Structure==

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[[Category: Single protein]]

[[Category: mRNA guanylyltransferase]]

[[Category: Doherty, A.J.]]

[[Category: Doherty, A J.]]

[[Category: Hakansson, K.]]

[[Category: Wigley, D.B.]]

[[Category: Wigley, D B.]]

[[Category: GTP]]

[[Category: capping enzyme]]

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[[Category: nucleotidyltransferase]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:01 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-We have solved the crystal structure of an mRNA capping enzyme at 2.5 A, resolution. The enzyme comprises two domains with a deep, but narrow, cleft between them. The two molecules in the crystallographic asymmetric, unit adopt very different conformations; both contain a bound GTP, but one, protein molecule is in an open conformation while the other is in a closed, conformation. Only in the closed conformation is the enzyme able to bind, manganese ions and undergo catalysis within the crystals to yield the, covalent guanylated enzyme intermediate. These structures provide direct, evidence for a mechanism that involves a significant conformational change, in the enzyme during catalysis.
+We have solved the crystal structure of an mRNA capping enzyme at 2.5 A resolution. The enzyme comprises two domains with a deep, but narrow, cleft between them. The two molecules in the crystallographic asymmetric unit adopt very different conformations; both contain a bound GTP, but one protein molecule is in an open conformation while the other is in a closed conformation. Only in the closed conformation is the enzyme able to bind manganese ions and undergo catalysis within the crystals to yield the covalent guanylated enzyme intermediate. These structures provide direct evidence for a mechanism that involves a significant conformational change in the enzyme during catalysis.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: mRNA guanylyltransferase]]
-[[Category: Doherty, A.J.]]
+[[Category: Doherty, A J.]]
 [[Category: Hakansson, K.]]
-[[Category: Wigley, D.B.]]
+[[Category: Wigley, D B.]]
 [[Category: GTP]]
 [[Category: capping enzyme]]
@@ Line 22: / Line 22: @@
 [[Category: nucleotidyltransferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:34:42 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:01 2008''