1kjj: Difference between revisions

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[[Image:1kjj.jpg|left|200px]]<br /><applet load="1kjj" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1kjj.jpg|left|200px]]
caption="1kjj, resolution 1.75&Aring;" />
 
'''Crystal structure of glycniamide ribonucleotide transformylase in complex with Mg-ATP-gamma-S'''<br />
{{Structure
|PDB= 1kjj |SIZE=350|CAPTION= <scene name='initialview01'>1kjj</scene>, resolution 1.75&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene> and <scene name='pdbligand=MPO:3[N-MORPHOLINO]PROPANE SULFONIC ACID'>MPO</scene>
|ACTIVITY=
|GENE= PURT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
}}
 
'''Crystal structure of glycniamide ribonucleotide transformylase in complex with Mg-ATP-gamma-S'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1KJJ 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=AGS:'>AGS</scene> and <scene name='pdbligand=MPO:'>MPO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KJJ OCA].  
1KJJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KJJ OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11953435 11953435]
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:[http://www.ncbi.nlm.nih.gov/pubmed/11953435 11953435]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 26: Line 35:
[[Category: purine biosynthesis]]
[[Category: purine biosynthesis]]


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Revision as of 10:18, 20 March 2008

File:1kjj.jpg


Drag the structure with the mouse to rotate
1kjj, resolution 1.75Å
Ligands: MG, NA, CL, AGS and MPO
Gene: PURT (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



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

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