1kjq: Difference between revisions
New page: left|200px<br /><applet load="1kjq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kjq, resolution 1.05Å" /> '''Crystal structure of... |
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[[Image:1kjq.jpg|left|200px]]<br /><applet load="1kjq" size=" | [[Image:1kjq.jpg|left|200px]]<br /><applet load="1kjq" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1kjq, resolution 1.05Å" /> | caption="1kjq, resolution 1.05Å" /> | ||
'''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== | ||
PurT-encoded glycinamide ribonucleotide transformylase, or PurT | 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== | ||
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:// | 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]] | ||
[[Category: Benkovic, S | [[Category: Benkovic, S J.]] | ||
[[Category: Firestine, S | [[Category: Firestine, S M.]] | ||
[[Category: Holden, H | [[Category: Holden, H M.]] | ||
[[Category: Thoden, J | [[Category: Thoden, J B.]] | ||
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: purine biosynthesis]] | [[Category: purine biosynthesis]] | ||
''Page seeded by [http:// | ''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
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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 MG, NA, CL, ADP, MPO and EDO 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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