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.

1oz0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1oz0.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1oz0.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1oz0| PDB=1oz0 | SCENE= }}
{{STRUCTURE_1oz0| PDB=1oz0 | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE HOMODIMERIC BIFUNCTIONAL TRANSFORMYLASE AND CYCLOHYDROLASE ENZYME AVIAN ATIC IN COMPLEX WITH A MULTISUBSTRATE ADDUCT INHIBITOR BETA-DADF.'''
+
===CRYSTAL STRUCTURE OF THE HOMODIMERIC BIFUNCTIONAL TRANSFORMYLASE AND CYCLOHYDROLASE ENZYME AVIAN ATIC IN COMPLEX WITH A MULTISUBSTRATE ADDUCT INHIBITOR BETA-DADF.===
-
==Overview==
+
<!--
-
The penultimate catalytic step of the purine de novo synthesis pathway is the conversion of aminoimidazole-4-carboxamide ribonucleotide (AICAR) to 5-formyl-AICAR that requires the cofactor N(10)-formyl-tetrahydrofolate as the formyl donor. This reaction is catalyzed by the AICAR transformylase domain of the bifunctional enzyme AICAR transformylase/inosine monophosphate cyclohydrolase (ATIC). Identification of the location of the AICAR transformylase active site was previously elucidated from the crystal structure of the avian ATIC with bound substrate AICAR; however, due to the absence of any bound folate, the folate binding region of the active site could not be identified. Here, we have determined the homodimeric crystal structure of avian ATIC in complex with the ATIC-specific multisubstrate adduct inhibitor beta-DADF to 2.5 A resolution. Beta-DADF encompasses both the AICAR and folate moieties into a single covalently linked entity, thereby allowing for the characterization of the folate binding pocket of the AICAR transformylase active site. Beta-DADF is intimately bound at the dimer interface of the transformylase domains with the majority of AICAR moiety interactions occurring within one subunit, whereas the primary interactions to the folate occur with the opposing subunit. The crystal structure suggests that a buried Lys(267) is transiently protonated during formyl transfer allowing for the stabilization of the oxyanion transition state and subsequent protonation of N10 on the tetrahydrofolate leaving group. Furthermore, the beta-DADF-bound structure provides a more optimal three-dimensional scaffold to improve the design of specific antineoplastic agents.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12974624}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12974624 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12974624}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Homodimer]]
[[Category: Homodimer]]
[[Category: Impch domain = alpha/beta/alpha]]
[[Category: Impch domain = alpha/beta/alpha]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:27:13 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:53:53 2008''

Revision as of 00:53, 29 July 2008

Image:1oz0.png

Template:STRUCTURE 1oz0

CRYSTAL STRUCTURE OF THE HOMODIMERIC BIFUNCTIONAL TRANSFORMYLASE AND CYCLOHYDROLASE ENZYME AVIAN ATIC IN COMPLEX WITH A MULTISUBSTRATE ADDUCT INHIBITOR BETA-DADF.

Template:ABSTRACT PUBMED 12974624

About this Structure

1OZ0 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Structure of avian AICAR transformylase with a multisubstrate adduct inhibitor beta-DADF identifies the folate binding site., Wolan DW, Greasley SE, Wall MJ, Benkovic SJ, Wilson IA, Biochemistry. 2003 Sep 23;42(37):10904-14. PMID:12974624

Page seeded by OCA on Tue Jul 29 03:53:53 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1oz0"
Personal tools