1EKS

ASP128ALA VARIANT OF MOAC PROTEIN FROM E. COLI

Summary for 1EKS

• Entry DOI: 10.2210/pdb1eks/pdb
• Related: 1EKR
• Descriptor: MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN C, L(+)-TARTARIC ACID (3 entities in total)
• Functional Keywords: moac, molybdenum cofactor (moco), moco biosynthesis, moco deficiency, translation
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 17583.35

Authors

Schindelin, H.,Liu, M.T.W.,Wuebbens, M.M.,Rajagopalan, K.V. (deposition date: 2000-03-09, release date: 2000-09-20, Last modification date: 2024-02-07)

Primary citation

Wuebbens, M.M.,Liu, M.T.,Rajagopalan, K.,Schindelin, H.
Insights into molybdenum cofactor deficiency provided by the crystal structure of the molybdenum cofactor biosynthesis protein MoaC.
Structure Fold.Des., 8:709-718, 2000

PubMed Abstract: 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.

PubMed: 10903949
DOI: 10.1016/S0969-2126(00)00157-X

Experimental method

X-RAY DIFFRACTION (2.5 Å)