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| - | [[Image:1kjq.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1kjq| PDB=1kjq | SCENE= }} | | {{STRUCTURE_1kjq| PDB=1kjq | SCENE= }} |
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| - | '''Crystal structure of glycinamide ribonucleotide transformylase in complex with Mg-ADP'''
| + | ===Crystal structure of glycinamide ribonucleotide transformylase in complex with Mg-ADP=== |
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| - | ==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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11953435}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11953435 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11953435}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Nucleotide]] | | [[Category: Nucleotide]] |
| | [[Category: Purine biosynthesis]] | | [[Category: Purine biosynthesis]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:49:33 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:26:28 2008'' |
Revision as of 07:26, 2 July 2008
Template:STRUCTURE 1kjq
Crystal structure of glycinamide ribonucleotide transformylase in complex with Mg-ADP
Template:ABSTRACT PUBMED 11953435
About this Structure
1KJQ is a Single protein structure of sequence from Escherichia coli. 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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