2ZQQ

Crystal structure of human AUH (3-methylglutaconyl-coa hydratase) mixed with (AUUU)24A RNA

Summary for 2ZQQ

• Entry DOI: 10.2210/pdb2zqq/pdb
• Related: 1HZD 1V4M 2E8K
• Descriptor: Methylglutaconyl-CoA hydratase (2 entities in total)
• Functional Keywords: beta spiral, lyase, branched-chain amino acid catabolism, disease mutation, mitochondrion, rna-binding, transit peptide, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion (By similarity): Q13825
• Total number of polymer chains: 6
• Total formula weight: 175428.92

Authors

Kurimoto, K.,Kuwasako, K.,Muto, Y.,Nureki, O.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2008-08-16, release date: 2009-06-30, Last modification date: 2023-11-01)

Primary citation

Kurimoto, K.,Kuwasako, K.,Sandercock, A.M.,Unzai, S.,Robinson, C.V.,Muto, Y.,Yokoyama, S.
AU-rich RNA-binding induces changes in the quaternary structure of AUH
Proteins, 75:360-372, 2009

PubMed Abstract: The human AU RNA binding protein/enoyl-Coenzyme A hydratase (AUH) is a 3-hydroxy-3-methylglutaconyl-CoA dehydratase in the leucine degradation pathway. It also possesses an RNA-binding activity to AUUU repeats, which involves no known conserved RNA-binding domains and is seemingly unrelated to the enzymatic activity. In this study, we performed mass spectrometric analyses to elucidate the oligomeric states of AUH in the presence and absence of RNA. With a short RNA (AUUU) or without RNA, AUH mainly exists as a trimer in solution. On the other hand, the AUH trimer dimerizes upon binding to one molecule of a long RNA containing 24 repeats of the AUUU motif, (AUUU)(24)A. AUH was crystallized with the long RNA. Although the RNA was disordered in the crystalline lattice, the AUH structure was determined as an asymmetric dimer of trimers with a kink in the alignment of the trimer axes, resulting in the formation of two clefts with significantly different sizes.

PubMed: 18831052
DOI: 10.1002/prot.22246

Experimental method

X-RAY DIFFRACTION (2.2 Å)