1kjj

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[[Image:1kjj.jpg|left|200px]]
[[Image:1kjj.jpg|left|200px]]
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{{Structure
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|PDB= 1kjj |SIZE=350|CAPTION= <scene name='initialview01'>1kjj</scene>, resolution 1.75&Aring;
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The line below this paragraph, containing "STRUCTURE_1kjj", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPO:3[N-MORPHOLINO]PROPANE+SULFONIC+ACID'>MPO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
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|GENE= PURT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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{{STRUCTURE_1kjj| PDB=1kjj | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kjj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kjj OCA], [http://www.ebi.ac.uk/pdbsum/1kjj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kjj RCSB]</span>
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'''Crystal structure of glycniamide ribonucleotide transformylase in complex with Mg-ATP-gamma-S'''
'''Crystal structure of glycniamide ribonucleotide transformylase in complex with Mg-ATP-gamma-S'''
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[[Category: Holden, H M.]]
[[Category: Holden, H M.]]
[[Category: Thoden, J B.]]
[[Category: Thoden, J B.]]
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[[Category: atp-grasp]]
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[[Category: Atp-grasp]]
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[[Category: nucleotide]]
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[[Category: Nucleotide]]
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[[Category: purine biosynthesis]]
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[[Category: Purine biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:49:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:49:28 2008''
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Revision as of 19:49, 2 May 2008

Template:STRUCTURE 1kjj

Crystal structure of glycniamide ribonucleotide transformylase in complex with Mg-ATP-gamma-S


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

1KJJ 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 Page seeded by OCA on Fri May 2 22:49:03 2008

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