This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1kjq
From Proteopedia
(New page: 200px<br /><applet load="1kjq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kjq, resolution 1.05Å" /> '''Crystal structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[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== | ||
| Line 13: | Line 13: | ||
[[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]] | ||
| Line 27: | Line 27: | ||
[[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
|
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
Page seeded by OCA on Thu Feb 21 13:34:51 2008
Categories: Escherichia coli | Single protein | Benkovic, S J. | Firestine, S M. | Holden, H M. | Thoden, J B. | ADP | CL | EDO | MG | MPO | NA | Atp-grasp | Nucleotide | Purine biosynthesis
