1eks
From Proteopedia
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'''ASP128ALA VARIANT OF MOAC PROTEIN FROM E. COLI''' | '''ASP128ALA VARIANT OF MOAC PROTEIN FROM E. COLI''' | ||
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[[Category: Schindelin, H.]] | [[Category: Schindelin, H.]] | ||
[[Category: Wuebbens, M M.]] | [[Category: Wuebbens, M M.]] | ||
| - | [[Category: | + | [[Category: Moac]] |
| - | [[Category: | + | [[Category: Moco biosynthesis]] |
| - | [[Category: | + | [[Category: Moco deficiency]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:13:21 2008'' | |
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Revision as of 12:13, 2 May 2008
ASP128ALA VARIANT OF MOAC PROTEIN FROM E. COLI
Overview
BACKGROUND: The molybdenum cofactor (Moco) is an essential component of a large family of enzymes involved in important transformations in carbon, nitrogen and sulfur metabolism. The Moco biosynthetic pathway is evolutionarily conserved and found in archaea, eubacteria and eukaryotes. In humans, genetic deficiencies of enzymes involved in this pathway trigger an autosomal recessive and usually deadly disease with severe neurological symptoms. The MoaC protein, together with the MoaA protein, is involved in the first step of Moco biosynthesis. RESULTS: MoaC from Escherichia coli has been expressed and purified to homogeneity and its crystal structure determined at 2 A resolution. The enzyme is organized into a tightly packed hexamer with 32 symmetry. The monomer consists of an antiparallel, four-stranded beta sheet packed against two long alpha helices, and its fold belongs to the ferredoxin-like family. Analysis of structural and biochemical data strongly suggests that the active site is located at the interface of two monomers in a pocket that contains several strictly conserved residues. CONCLUSIONS: Asp128 in the putative active site appears to be important for catalysis as its replacement with alanine almost completely abolishes protein activity. The structure of the Asp128-->Ala variant reveals substantial conformational changes in an adjacent loop. In the human MoaC ortholog, substitution of Thr182 with proline causes Moco deficiency, and the corresponding substitution in MoaC severely compromises activity. This residue is located near the N-terminal end of helix alpha4 at an interface between two monomers. The MoaC structure provides a framework for the analysis of additional dysfunctional mutations in the corresponding human gene.
About this Structure
1EKS is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Insights into molybdenum cofactor deficiency provided by the crystal structure of the molybdenum cofactor biosynthesis protein MoaC., Wuebbens MM, Liu MT, Rajagopalan K, Schindelin H, Structure. 2000 Jul 15;8(7):709-18. PMID:10903949 Page seeded by OCA on Fri May 2 15:13:21 2008
