3ZXS

Cryptochrome B from Rhodobacter sphaeroides

Summary for 3ZXS

• Entry DOI: 10.2210/pdb3zxs/pdb
• Descriptor: CRYPTOCHROME B, FLAVIN-ADENINE DINUCLEOTIDE, IRON/SULFUR CLUSTER, ... (7 entities in total)
• Functional Keywords: lyase, crypro, lumazine, iron-sulfur-cluster
• Biological source: RHODOBACTER SPHAEROIDES
• Total number of polymer chains: 3
• Total formula weight: 184420.29

Authors

Geisselbrecht, Y.,Fruhwirth, S.,Pierik, A.J.,Klug, G.,Essen, L.-O. (deposition date: 2011-08-15, release date: 2012-02-15, Last modification date: 2024-05-08)

Primary citation

Geisselbrecht, Y.,Fruhwirth, S.,Schroeder, C.,Pierik, A.J.,Klug, G.,Essen, L.-O.
Cryb from Rhodobacter Sphaeroides: A Unique Class of Cryptochromes with New Cofactors.
Embo Rep., 13:223-, 2012

PubMed Abstract: Cryptochromes and photolyases are structurally related but have different biological functions in signalling and DNA repair. Proteobacteria and cyanobacteria harbour a new class of cryptochromes, called CryPro. We have solved the 2.7 Å structure of one of its members, cryptochrome B from Rhodobacter sphaeroides, which is a regulator of photosynthesis gene expression. The structure reveals that, in addition to the photolyase-like fold, CryB contains two cofactors only conserved in the CryPro subfamily: 6,7-dimethyl-8-ribityl-lumazine in the antenna-binding domain and a [4Fe-4S] cluster within the catalytic domain. The latter closely resembles the iron-sulphur cluster harbouring the large primase subunit PriL, indicating that PriL is evolutionarily related to the CryPro class of cryptochromes.

PubMed: 22290493
DOI: 10.1038/EMBOR.2012.2

Experimental method

X-RAY DIFFRACTION (2.7 Å)