4ZOH

Crystal structure of glyceraldehyde oxidoreductase

Summary for 4ZOH

• Entry DOI: 10.2210/pdb4zoh/pdb
• Descriptor: Putative oxidoreductase molybdopterin-binding subunit, ACETIC ACID, FE2/S2 (INORGANIC) CLUSTER, ... (12 entities in total)
• Functional Keywords: xanthine oxidoreductase family, molybdopterin cofactor, flavin adenine dinucleotide, iron-sulfur cluster, oxidoreductase
• Biological source: Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7); More
• Total number of polymer chains: 3
• Total formula weight: 130095.38

Authors

Nishimasu, H.,Fushinobu, S.,Wakagi, T. (deposition date: 2015-05-06, release date: 2016-02-03, Last modification date: 2024-10-16)

Primary citation

Wakagi, T.,Nishimasu, H.,Miyake, M.,Fushinobu, S.
Archaeal Mo-Containing Glyceraldehyde Oxidoreductase Isozymes Exhibit Diverse Substrate Specificities through Unique Subunit Assemblies.
Plos One, 11:e0147333-e0147333, 2016

PubMed Abstract: Archaea use glycolytic pathways distinct from those found in bacteria and eukaryotes, where unique enzymes catalyze each reaction step. In this study, we isolated three isozymes of glyceraldehyde oxidoreductase (GAOR1, GAOR2 and GAOR3) from the thermoacidophilic archaeon Sulfolobus tokodaii. GAOR1-3 belong to the xanthine oxidoreductase superfamily, and are composed of a molybdo-pyranopterin subunit (L), a flavin subunit (M), and an iron-sulfur subunit (S), forming an LMS hetero-trimer unit. We found that GAOR1 is a tetramer of the STK17810/STK17830/STK17820 hetero-trimer, GAOR2 is a dimer of the STK23390/STK05620/STK05610 hetero-trimer, and GAOR3 is the STK24840/STK05620/STK05610 hetero-trimer. GAOR1-3 exhibited diverse substrate specificities for their electron donors and acceptors, due to their different L-subunits, and probably participate in the non-phosphorylative Entner-Doudoroff glycolytic pathway. We determined the crystal structure of GAOR2, as the first three-dimensional structure of an archaeal molybdenum-containing hydroxylase, to obtain structural insights into their substrate specificities and subunit assemblies. The gene arrangement and the crystal structure suggested that the M/S-complex serves as a structural scaffold for the binding of the L-subunit, to construct the three enzymes with different specificities. Collectively, our findings illustrate a novel principle of a prokaryotic multicomponent isozyme system.

PubMed: 26808202
DOI: 10.1371/journal.pone.0147333

Experimental method

X-RAY DIFFRACTION (2.2 Å)