3TD7

Crysal structure of the mimivirus sulfhydryl oxidase R596

Summary for 3TD7

• Entry DOI: 10.2210/pdb3td7/pdb
• Related: 3GWL 3GWN 3P0K
• Descriptor: FAD-linked sulfhydryl oxidase R596, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: four helix-bundle, orfan domain, oxidase, oxidoreductase
• Biological source: Acanthamoeba polyphaga mimivirus (APMV)
• Cellular location: Virion : Q5UP54
• Total number of polymer chains: 1
• Total formula weight: 34988.42

Authors

Hakim, M.,Fass, D. (deposition date: 2011-08-10, release date: 2012-09-05, Last modification date: 2024-10-30)

Primary citation

Hakim, M.,Ezerina, D.,Alon, A.,Vonshak, O.,Fass, D.
Exploring ORFan domains in giant viruses: structure of mimivirus sulfhydryl oxidase R596.
Plos One, 7:e50649-e50649, 2012

PubMed Abstract: The mimivirus genome contains many genes that lack homologs in the sequence database and are thus known as ORFans. In addition, mimivirus genes that encode proteins belonging to known fold families are in some cases fused to domain-sized segments that cannot be classified. One such ORFan region is present in the mimivirus enzyme R596, a member of the Erv family of sulfhydryl oxidases. We determined the structure of a variant of full-length R596 and observed that the carboxy-terminal region of R596 assumes a folded, compact domain, demonstrating that these ORFan segments can be stable structural units. Moreover, the R596 ORFan domain fold is novel, hinting at the potential wealth of protein structural innovation yet to be discovered in large double-stranded DNA viruses. In the context of the R596 dimer, the ORFan domain contributes to formation of a broad cleft enriched with exposed aromatic groups and basic side chains, which may function in binding target proteins or localization of the enzyme within the virus factory or virions. Finally, we find evidence for an intermolecular dithiol/disulfide relay within the mimivirus R596 dimer, the first such extended, intersubunit redox-active site identified in a viral sulfhydryl oxidase.

PubMed: 23209798
DOI: 10.1371/journal.pone.0050649

Experimental method

X-RAY DIFFRACTION (2.21 Å)