1ulz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ulz.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ulz.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ulz| PDB=1ulz | SCENE= }}
{{STRUCTURE_1ulz| PDB=1ulz | SCENE= }}
-
'''Crystal structure of the biotin carboxylase subunit of pyruvate carboxylase'''
+
===Crystal structure of the biotin carboxylase subunit of pyruvate carboxylase===
-
==Overview==
+
<!--
-
Pyruvate carboxylase (PC) is distributed in many eukaryotes as well as in some prokaryotes. PC catalyzes the ATP-dependent carboxylation of pyruvate to form oxalacetate. PC has three functional domains, one of which is a biotin carboxylase (BC) domain. The BC subunit of PC from Aquifex aeolicus (PC-beta) was crystallized in an orthorhombic form with space group P2(1)2(1)2, unit-cell parameters a = 92.4, b = 122.1, c = 59.0 A and one molecule in the asymmetric unit. Diffraction data were collected at 100 K on BL24XU at SPring-8. The crystal structure was determined by the molecular-replacement method and refined against 20.0-2.2 A resolution data, giving an R factor of 0.199 and a free R factor of 0.236. The crystal structure revealed that PC-beta forms a dimeric quaternary structure consisting of two molecules related by crystallographic twofold symmetry. The overall structure of PC-beta is similar to other biotin-dependent carboxylases, such as acetyl-CoA carboxylase (ACC). Although some parts of domain B were disordered in ACC, the corresponding parts of PC-beta were clearly determined in the crystal structure. From comparison between the active-site structure of ACC with ATP bound and a virtual model of PC-beta with ATP bound, it was shown that the backbone torsion angles of Glu203 in PC-beta change and some of water molecules in the active site of PC-beta are excluded upon ATP binding.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14993673}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14993673 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14993673}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Biotin carboxylase]]
[[Category: Biotin carboxylase]]
[[Category: Pyruvate carboxylase]]
[[Category: Pyruvate carboxylase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:24:39 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:34:19 2008''

Revision as of 21:34, 28 July 2008

Template:STRUCTURE 1ulz

Crystal structure of the biotin carboxylase subunit of pyruvate carboxylase

Template:ABSTRACT PUBMED 14993673

About this Structure

1ULZ is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.

Reference

Structure of the biotin carboxylase subunit of pyruvate carboxylase from Aquifex aeolicus at 2.2 A resolution., Kondo S, Nakajima Y, Sugio S, Yong-Biao J, Sueda S, Kondo H, Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):486-92. Epub 2004, Feb 25. PMID:14993673

Page seeded by OCA on Tue Jul 29 00:34:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools