1ulz
From Proteopedia
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| - | [[Image:1ulz.gif|left|200px]] | + | [[Image:1ulz.gif|left|200px]] |
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| - | '''Crystal structure of the biotin carboxylase subunit of pyruvate carboxylase''' | + | {{Structure |
| + | |PDB= 1ulz |SIZE=350|CAPTION= <scene name='initialview01'>1ulz</scene>, resolution 2.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Pyruvate_carboxylase Pyruvate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.1 6.4.1.1] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the biotin carboxylase subunit of pyruvate carboxylase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ULZ is a [ | + | 1ULZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULZ OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14993673 14993673] |
[[Category: Aquifex aeolicus]] | [[Category: Aquifex aeolicus]] | ||
[[Category: Pyruvate carboxylase]] | [[Category: Pyruvate carboxylase]] | ||
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[[Category: pyruvate carboxylase]] | [[Category: pyruvate carboxylase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:33:44 2008'' |
Revision as of 12:33, 20 March 2008
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| , resolution 2.2Å | |||||||
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| Activity: | Pyruvate carboxylase, with EC number 6.4.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
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
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