1HZD

CRYSTAL STRUCTURE OF HUMAN AUH PROTEIN, AN RNA-BINDING HOMOLOGUE OF ENOYL-COA HYDRATASE

Summary for 1HZD

• Entry DOI: 10.2210/pdb1hzd/pdb
• Related: 1DCI 1DUB
• Descriptor: AU-BINDING PROTEIN/ENOYL-COA HYDRATASE (2 entities in total)
• Functional Keywords: rna-binding protein, enoyl-coa hydratase, riken structural genomics/proteomics initiative, rsgi, structural genomics, lyase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 6
• Total formula weight: 175428.92

Authors

Kurimoto, K.,Fukai, S.,Nureki, O.,Muto, Y.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2001-01-24, release date: 2001-12-12, Last modification date: 2023-08-09)

Primary citation

Kurimoto, K.,Fukai, S.,Nureki, O.,Muto, Y.,Yokoyama, S.
Crystal structure of human AUH protein, a single-stranded RNA binding homolog of enoyl-CoA hydratase.
Structure, 9:1253-1263, 2001

PubMed Abstract: The AU binding homolog of enoyl-CoA hydratase (AUH) is a bifunctional protein that has two distinct activities: AUH binds to RNA and weakly catalyzes the hydration of 2-trans-enoyl-coenzyme A (enoyl-CoA). AUH has no sequence similarity with other known RNA binding proteins, but it has considerable sequence similarity with enoyl-CoA hydratase. A segment of AUH, named the R peptide, binds to RNA. However, the mechanism of the RNA binding activity of AUH remains to be elucidated.

PubMed: 11738050
DOI: 10.1016/S0969-2126(01)00686-4

Experimental method

X-RAY DIFFRACTION (2.2 Å)