1kji: Difference between revisions

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[[Image:1kji.jpg|left|200px]]<br /><applet load="1kji" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1kji.jpg|left|200px]]<br /><applet load="1kji" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1kji, resolution 1.60Å" />

'''Crystal structure of glycinamide ribonucleotide transformylase in complex with Mg-AMPPCP'''<br />

==Overview==

PurT-encoded glycinamide ribonucleotide transformylase, or PurT, transformylase, functions in purine biosynthesis by catalyzing the, formylation of glycinamide ribonucleotide through a catalytic mechanism, requiring Mg(2+)ATP and formate. From previous x-ray diffraction analyses, it has been demonstrated that PurT transformylase from Escherichia coli, belongs to the ATP-grasp superfamily of enzymes, which are characterized, by three structural motifs referred to as the A-, B-, and C-domains. In, all of the ATP-grasp enzymes studied to date, the adenosine nucleotide, ligands are invariably wedged between the B- and C-domains, and in some, cases, such as biotin carboxylase and carbamoyl phosphate synthetase, the, B-domains move significantly upon nucleotide binding. Here we present a, systematic and high-resolution structural investigation of PurT, transformylase complexed with various adenosine nucleotides or nucleotide, analogs including Mg(2+)ATP, Mg(2+)-5'-adenylylimidodiphosphate, Mg(2+)-beta,gamma-methyleneadenosine 5'-triphosphate, Mg(2+)ATPgammaS, or, Mg(2+)ADP. Taken together, these studies indicate that the conformation of, the so-called "T-loop," delineated by Lys-155 to Gln-165, is highly, sensitive to the chemical identity of the nucleotide situated in the, binding pocket. This sensitivity to nucleotide identity is in sharp, contrast to that observed for the "P-loop"-containing enzymes, in which, the conformation of the binding motif is virtually unchanged in the, presence or absence of nucleotides.

PurT-encoded glycinamide ribonucleotide transformylase, or PurT transformylase, functions in purine biosynthesis by catalyzing the formylation of glycinamide ribonucleotide through a catalytic mechanism requiring Mg(2+)ATP and formate. From previous x-ray diffraction analyses, it has been demonstrated that PurT transformylase from Escherichia coli belongs to the ATP-grasp superfamily of enzymes, which are characterized by three structural motifs referred to as the A-, B-, and C-domains. In all of the ATP-grasp enzymes studied to date, the adenosine nucleotide ligands are invariably wedged between the B- and C-domains, and in some cases, such as biotin carboxylase and carbamoyl phosphate synthetase, the B-domains move significantly upon nucleotide binding. Here we present a systematic and high-resolution structural investigation of PurT transformylase complexed with various adenosine nucleotides or nucleotide analogs including Mg(2+)ATP, Mg(2+)-5'-adenylylimidodiphosphate, Mg(2+)-beta,gamma-methyleneadenosine 5'-triphosphate, Mg(2+)ATPgammaS, or Mg(2+)ADP. Taken together, these studies indicate that the conformation of the so-called "T-loop," delineated by Lys-155 to Gln-165, is highly sensitive to the chemical identity of the nucleotide situated in the binding pocket. This sensitivity to nucleotide identity is in sharp contrast to that observed for the "P-loop"-containing enzymes, in which the conformation of the binding motif is virtually unchanged in the presence or absence of nucleotides.

==About this Structure==

1KJI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG, NA, CL, ACP, MPO and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1KJI OCA].

1KJI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=ACP:'>ACP</scene>, <scene name='pdbligand=MPO:'>MPO</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KJI OCA].

==Reference==

Line 13:

[[Category: Escherichia coli]]

[[Category: Single protein]]

[[Category: Benkovic, S.J.]]

[[Category: Benkovic, S J.]]

[[Category: Firestine, S.M.]]

[[Category: Firestine, S M.]]

[[Category: Holden, H.M.]]

[[Category: Holden, H M.]]

[[Category: Thoden, J.B.]]

[[Category: Thoden, J B.]]

[[Category: ACP]]

[[Category: CL]]

Line 27:

[[Category: purine biosynthesis]]

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@@ Line 1: / Line 1: @@
-[[Image:1kji.jpg|left|200px]]<br /><applet load="1kji" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1kji.jpg|left|200px]]<br /><applet load="1kji" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1kji, resolution 1.60&Aring;" />
 '''Crystal structure of glycinamide ribonucleotide transformylase in complex with Mg-AMPPCP'''<br />
 ==Overview==
-PurT-encoded glycinamide ribonucleotide transformylase, or PurT, transformylase, functions in purine biosynthesis by catalyzing the, formylation of glycinamide ribonucleotide through a catalytic mechanism, requiring Mg(2+)ATP and formate. From previous x-ray diffraction analyses, it has been demonstrated that PurT transformylase from Escherichia coli, belongs to the ATP-grasp superfamily of enzymes, which are characterized, by three structural motifs referred to as the A-, B-, and C-domains. In, all of the ATP-grasp enzymes studied to date, the adenosine nucleotide, ligands are invariably wedged between the B- and C-domains, and in some, cases, such as biotin carboxylase and carbamoyl phosphate synthetase, the, B-domains move significantly upon nucleotide binding. Here we present a, systematic and high-resolution structural investigation of PurT, transformylase complexed with various adenosine nucleotides or nucleotide, analogs including Mg(2+)ATP, Mg(2+)-5'-adenylylimidodiphosphate, Mg(2+)-beta,gamma-methyleneadenosine 5'-triphosphate, Mg(2+)ATPgammaS, or, Mg(2+)ADP. Taken together, these studies indicate that the conformation of, the so-called "T-loop," delineated by Lys-155 to Gln-165, is highly, sensitive to the chemical identity of the nucleotide situated in the, binding pocket. This sensitivity to nucleotide identity is in sharp, contrast to that observed for the "P-loop"-containing enzymes, in which, the conformation of the binding motif is virtually unchanged in the, presence or absence of nucleotides.
+PurT-encoded glycinamide ribonucleotide transformylase, or PurT transformylase, functions in purine biosynthesis by catalyzing the formylation of glycinamide ribonucleotide through a catalytic mechanism requiring Mg(2+)ATP and formate. From previous x-ray diffraction analyses, it has been demonstrated that PurT transformylase from Escherichia coli belongs to the ATP-grasp superfamily of enzymes, which are characterized by three structural motifs referred to as the A-, B-, and C-domains. In all of the ATP-grasp enzymes studied to date, the adenosine nucleotide ligands are invariably wedged between the B- and C-domains, and in some cases, such as biotin carboxylase and carbamoyl phosphate synthetase, the B-domains move significantly upon nucleotide binding. Here we present a systematic and high-resolution structural investigation of PurT transformylase complexed with various adenosine nucleotides or nucleotide analogs including Mg(2+)ATP, Mg(2+)-5'-adenylylimidodiphosphate, Mg(2+)-beta,gamma-methyleneadenosine 5'-triphosphate, Mg(2+)ATPgammaS, or Mg(2+)ADP. Taken together, these studies indicate that the conformation of the so-called "T-loop," delineated by Lys-155 to Gln-165, is highly sensitive to the chemical identity of the nucleotide situated in the binding pocket. This sensitivity to nucleotide identity is in sharp contrast to that observed for the "P-loop"-containing enzymes, in which the conformation of the binding motif is virtually unchanged in the presence or absence of nucleotides.
 ==About this Structure==
-KJI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG, NA, CL, ACP, MPO and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KJI OCA].
+KJI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=ACP:'>ACP</scene>, <scene name='pdbligand=MPO:'>MPO</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KJI OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Benkovic, S.J.]]
+[[Category: Benkovic, S J.]]
-[[Category: Firestine, S.M.]]
+[[Category: Firestine, S M.]]
-[[Category: Holden, H.M.]]
+[[Category: Holden, H M.]]
-[[Category: Thoden, J.B.]]
+[[Category: Thoden, J B.]]
 [[Category: ACP]]
 [[Category: CL]]
@@ Line 27: / Line 27: @@
 [[Category: purine biosynthesis]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:17:21 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:34:47 2008''