This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1rb0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1rb0.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1rb0.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1rb0| PDB=1rb0 | SCENE= }}
{{STRUCTURE_1rb0| PDB=1rb0 | SCENE= }}
-
'''CRYSTAL STRUCTURE OF A BINARY COMPLEX OF E. COLI HPPK WITH 6-HYDROXYMETHYLPTERIN-DIPHOSPHATE AT 1.35 ANGSTROM RESOLUTION'''
+
===CRYSTAL STRUCTURE OF A BINARY COMPLEX OF E. COLI HPPK WITH 6-HYDROXYMETHYLPTERIN-DIPHOSPHATE AT 1.35 ANGSTROM RESOLUTION===
-
==Overview==
+
<!--
-
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) catalyzes the Mg(2+)-dependent pyrophosphoryl transfer from ATP to 6-hydroxymethyl-7,8-dihydropterin (HP). The reaction follows a bi-bi mechanism with ATP as the first substrate and AMP and HP pyrophosphate (HPPP) as the two products. HPPK is a key enzyme in the folate biosynthetic pathway and is essential for microorganisms but absent from mammals. For the HPPK-catalyzed pyrophosphoryl transfer, a reaction coordinate is constructed on the basis of the thermodynamic and transient kinetic data we reported previously, and the reaction trajectory is mapped out with five three-dimensional structures of the enzyme at various liganded states. The five structures are apo-HPPK (ligand-free enzyme), HPPK.MgATP(analog) (binary complex of HPPK with its first substrate) and HPPK.MgATP(analog).HP (ternary complex of HPPK with both substrates), which we reported previously, and HPPK.AMP.HPPP (ternary complex of HPPK with both product molecules) and HPPK.HPPP (binary complex of HPPK with one product), which we present in this study.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15016362}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15016362 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15016362}}
==About this Structure==
==About this Structure==
Line 40: Line 44:
[[Category: Ternary complex]]
[[Category: Ternary complex]]
[[Category: X-ray crystallography]]
[[Category: X-ray crystallography]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:17:23 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:37:59 2008''

Revision as of 22:38, 28 July 2008

Image:1rb0.png

Template:STRUCTURE 1rb0

CRYSTAL STRUCTURE OF A BINARY COMPLEX OF E. COLI HPPK WITH 6-HYDROXYMETHYLPTERIN-DIPHOSPHATE AT 1.35 ANGSTROM RESOLUTION

Template:ABSTRACT PUBMED 15016362

About this Structure

1RB0 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Reaction trajectory of pyrophosphoryl transfer catalyzed by 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase., Blaszczyk J, Shi G, Li Y, Yan H, Ji X, Structure. 2004 Mar;12(3):467-75. PMID:15016362

Page seeded by OCA on Tue Jul 29 01:37:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rb0"
Personal tools