3bg3

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{{STRUCTURE_3bg3| PDB=3bg3 | SCENE= }}
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'''Crystal Structure of Human Pyruvate Carboxylase (missing the biotin carboxylase domain at the N-terminus)'''
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===Crystal Structure of Human Pyruvate Carboxylase (missing the biotin carboxylase domain at the N-terminus)===
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==Overview==
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Pyruvate carboxylase (PC) catalyzes the biotin-dependent production of oxaloacetate and has important roles in gluconeogenesis, lipogenesis, insulin secretion and other cellular processes. PC contains the biotin carboxylase (BC), carboxyltransferase (CT) and biotin-carboxyl carrier protein (BCCP) domains. We report here the crystal structures at 2.8-A resolution of full-length PC from Staphylococcus aureus and the C-terminal region (missing only the BC domain) of human PC. A conserved tetrameric association is observed for both enzymes, and our structural and mutagenesis studies reveal a previously uncharacterized domain, the PC tetramerization (PT) domain, which is important for oligomerization. A BCCP domain is located in the active site of the CT domain, providing the first molecular insights into how biotin participates in the carboxyltransfer reaction. There are dramatic differences in domain positions in the monomer and the organization of the tetramer between these enzymes and the PC from Rhizobium etli.
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{{ABSTRACT_PUBMED_18297087}}
==Disease==
==Disease==
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[[Category: Tim barrel]]
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[[Category: Transit peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:38:42 2008''

Revision as of 13:38, 29 July 2008

Image:3bg3.png

Template:STRUCTURE 3bg3

Contents

Crystal Structure of Human Pyruvate Carboxylase (missing the biotin carboxylase domain at the N-terminus)

Template:ABSTRACT PUBMED 18297087

Disease

Known disease associated with this structure: Pyruvate carboxylase deficiency OMIM:[608786]

About this Structure

3BG3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction., Xiang S, Tong L, Nat Struct Mol Biol. 2008 Mar;15(3):295-302. Epub 2008 Feb 24. PMID:18297087

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