Journal of Structural and Functional Genomics

, Volume 14, Issue 3, pp 119–126 | Cite as

Solution NMR structures provide first structural coverage of the large protein domain family PF08369 and complementary structural coverage of dark operative protochlorophyllide oxidoreductase complexes

  • Surya V. S. R. K. Pulavarti
  • Yunfen He
  • Erik A. Feldmann
  • Alexander Eletsky
  • Thomas B. Acton
  • Rong Xiao
  • John K. Everett
  • Gaetano T. Montelione
  • Michael A. KennedyEmail author
  • Thomas SzyperskiEmail author


High-quality NMR structures of the C-terminal domain comprising residues 484–537 of the 537-residue protein Bacterial chlorophyll subunit B (BchB) from Chlorobium tepidum and residues 9–61 of 61-residue Asr4154 from Nostoc sp. (strain PCC 7120) exhibit a mixed α/β fold comprised of three α-helices and a small β-sheet packed against second α-helix. These two proteins share 29 % sequence similarity and their structures are globally quite similar. The structures of BchB(484–537) and Asr4154(9–61) are the first representative structures for the large protein family (Pfam) PF08369, a family of unknown function currently containing 610 members in bacteria and eukaryotes. Furthermore, BchB(484–537) complements the structural coverage of the dark-operating protochlorophyllide oxidoreductase.


BchB DPOR Asr4154 PF08369 PCP-red Structural genomics 



Bacterial chlorophyll subunit B


Bacterial chlorophyll subunit N


Chlorophyll subunit N


Chlorophyll subunit B


Dark-operative protochlorophyllide oxidoreductase


4,4-Dimethyl-4-silapentane-1-sulfonate sodium salt




2-(N-morpholino)ethanesulfonic acid


Northeast Structural Genomics Consortium


Nuclear overhauser effect


Protochlorophyllide reductase


Protein Data Bank


Root mean square deviation



We thank Dr. Donald Petrey, Columbia University, for helpful discussions. This work was supported by the National Institutes of Health, grant number: U54 GM094597 (T.S., M.K. and G.T.M.).

Supplementary material

10969_2013_9159_MOESM1_ESM.pdf (1 mb)
Supplementary material 1 (PDF 1,040 kb)


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Copyright information

© Springer Science+Business Media Dordrecht 2013

Authors and Affiliations

  • Surya V. S. R. K. Pulavarti
    • 1
    • 2
  • Yunfen He
    • 1
    • 2
  • Erik A. Feldmann
    • 3
    • 4
  • Alexander Eletsky
    • 1
    • 2
  • Thomas B. Acton
    • 5
    • 6
  • Rong Xiao
    • 5
    • 6
  • John K. Everett
    • 5
    • 6
  • Gaetano T. Montelione
    • 5
    • 6
    • 7
  • Michael A. Kennedy
    • 3
    • 4
    Email author
  • Thomas Szyperski
    • 1
    • 2
    Email author
  1. 1.Department of ChemistryThe State University of New York at BuffaloBuffaloUSA
  2. 2.Northeast Structural Genomics ConsortiumBuffaloUSA
  3. 3.Department of Chemistry and BiochemistryMiami UniversityOxfordUSA
  4. 4.Northeast Structural Genomics ConsortiumOxfordUSA
  5. 5.Center of Advanced Biotechnology and Medicine and Department of Molecular Biology and Biochemistry, RutgersThe State University of New JerseyPiscatawayUSA
  6. 6.Northeast Structural Genomics ConsortiumPiscatawayUSA
  7. 7.Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical SchoolUMDNJPiscatawayUSA

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