1kjq

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(New page: 200px<br /><applet load="1kjq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kjq, resolution 1.05&Aring;" /> '''Crystal structure of...)
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'''Crystal structure of glycinamide ribonucleotide transformylase in complex with Mg-ADP'''<br />
'''Crystal structure of glycinamide ribonucleotide transformylase in complex with Mg-ADP'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1KJQ 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, ADP, 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=1KJQ OCA].
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1KJQ 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=ADP:'>ADP</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=1KJQ OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Benkovic, S.J.]]
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[[Category: Benkovic, S J.]]
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[[Category: Firestine, S.M.]]
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[[Category: Firestine, S M.]]
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[[Category: Holden, H.M.]]
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[[Category: Holden, H M.]]
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[[Category: Thoden, J.B.]]
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[[Category: Thoden, J B.]]
[[Category: ADP]]
[[Category: ADP]]
[[Category: CL]]
[[Category: CL]]
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[[Category: purine biosynthesis]]
[[Category: purine biosynthesis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:17:51 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:34:51 2008''

Revision as of 11:34, 21 February 2008

Image:1kjq.jpg

1kjq, resolution 1.05Å

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Crystal structure of glycinamide ribonucleotide transformylase in complex with Mg-ADP

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.

About this Structure

1KJQ is a Single protein structure of sequence from Escherichia coli with , , , , and as ligands. Full crystallographic information is available from OCA.

Reference

PurT-encoded glycinamide ribonucleotide transformylase. Accommodation of adenosine nucleotide analogs within the active site., Thoden JB, Firestine SM, Benkovic SJ, Holden HM, J Biol Chem. 2002 Jun 28;277(26):23898-908. Epub 2002 Apr 12. PMID:11953435

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