5YLY

Crystal structure of the cytochrome b5 reductase domain of Ulva prolifera nitrate reductase

Summary for 5YLY

• Entry DOI: 10.2210/pdb5yly/pdb
• Descriptor: Nitrate reductase, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: cytochrome b5 reductase domain, fad, ulva prolifera, nitrate reductase, flavoprotein
• Biological source: Ulva prolifera
• Total number of polymer chains: 2
• Total formula weight: 66636.26

Authors

Ma, Q.,You, C. (deposition date: 2017-10-20, release date: 2018-05-23, Last modification date: 2024-03-06)

Primary citation

You, C.,Liu, C.,Li, Y.,Jiang, P.,Ma, Q.
Structural and enzymatic analysis of the cytochrome b5reductase domain of Ulva prolifera nitrate reductase.
Int. J. Biol. Macromol., 111:1175-1182, 2018

PubMed Abstract: Rapid accumulations of unattached green macroalgae, referred to as blooms, constitute ecological disasters and occur in many coastal regions. Ulva are a major cause of blooms, owing to their high nitrogen utilization capacity, which requires nitrate reductase (NR) activity; however, molecular characterization of Ulva NR remains lacking. Herein we determined the crystal structure and performed an enzymatic analysis of the cytochrome b reductase domain of Ulva prolifera NR (UpCbRNR). The structural analysis revealed an N-terminal FAD-binding domain primarily consisting of six antiparallel β strands, a C-terminal NADH-binding domain forming a Rossmann fold, and a three β-stranded linker region connecting these two domains. The FAD cofactor was located in the cleft between the two domains and interacted primarily with the FAD-binding domain. UpCbRNR shares similarities in overall structure and cofactor interactions with homologs, and its catalytic ability is comparable to that of higher plant CbRNRs. Structure and sequence comparisons of homologs revealed two regions of sequence length variation potentially useful for phylogenetic analysis: one in the FAD-binding domain, specific to U. prolifera, and another in the linker region that may be used to differentiate between plant, fungi, and animal homologs. Our data will facilitate molecular-level understanding of nitrate assimilation in Ulva.

PubMed: 29371148
DOI: 10.1016/j.ijbiomac.2018.01.140

Experimental method

X-RAY DIFFRACTION (1.76 Å)