1DTW

HUMAN BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE

Summary for 1DTW

• Entry DOI: 10.2210/pdb1dtw/pdb
• Descriptor: BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE ALPHA SUBUNIT, BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE BETA SUBUNIT, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: thdp-binding fold, branched-chain alpha-keto acid dehydrogenase, oxidoreductase
• Biological source: Homo sapiens (human); More
• Cellular location: Mitochondrion matrix: P12694 P21953
• Total number of polymer chains: 2
• Total formula weight: 84001.18

Authors

AEvarsson, A.,Chuang, J.L.,Wynn, R.M.,Turley, S.,Chuang, D.T.,Hol, W.G.J. (deposition date: 2000-01-13, release date: 2000-03-27, Last modification date: 2024-02-07)

Primary citation

AEvarsson, A.,Chuang, J.L.,Wynn, R.M.,Turley, S.,Chuang, D.T.,Hol, W.G.
Crystal structure of human branched-chain alpha-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease.
Structure Fold.Des., 8:277-291, 2000

PubMed Abstract: Mutations in components of the extraordinarily large alpha-ketoacid dehydrogenase multienzyme complexes can lead to serious and often fatal disorders in humans, including maple syrup urine disease (MSUD). In order to obtain insight into the effect of mutations observed in MSUD patients, we determined the crystal structure of branched-chain alpha-ketoacid dehydrogenase (E1), the 170 kDa alpha(2)beta(2) heterotetrameric E1b component of the branched-chain alpha-ketoacid dehydrogenase multienzyme complex.

PubMed: 10745006
DOI: 10.1016/S0969-2126(00)00105-2

Experimental method

X-RAY DIFFRACTION (2.7 Å)