We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1kjq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1kjq.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1kjq.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1kjq| PDB=1kjq | SCENE= }}
{{STRUCTURE_1kjq| PDB=1kjq | SCENE= }}
-
'''Crystal structure of glycinamide ribonucleotide transformylase in complex with Mg-ADP'''
+
===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.
+
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.
 +
-->
 +
{{ABSTRACT_PUBMED_11953435}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[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

Image:1kjq.png

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

Page seeded by OCA on Wed Jul 2 10:26:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kjq"
Personal tools