1B3I

NMR SOLUTION STRUCTURE OF PLASTOCYANIN FROM THE PHOTOSYNTHETIC PROKARYOTE, PROCHLOROTHRIX HOLLANDICA (MINIMIZED AVERAGE STRUCTURE)


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 40 
  • Conformers Submitted: 
  • Selection Criteria: LOWEST TARGET FUNCTION 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

NMR solution structure of plastocyanin from the photosynthetic prokaryote, Prochlorothrix hollandica.

Babu, C.R.Volkman, B.F.Bullerjahn, G.S.

(1999) Biochemistry 38: 4988-4995

  • DOI: https://doi.org/10.1021/bi983024f
  • Primary Citation of Related Structures:  
    1B3I, 2B3I

  • PubMed Abstract: 

    The solution structure of a divergent plastocyanin (PC) from the photosynthetic prokaryote Prochlorothrix hollandica was determined by homonuclear 1H NMR spectroscopy. Nineteen structures were calculated from 1222 distance restraints, yielding a family of structures having an average rmsd of 0.42 +/- 0.08 A for backbone atoms and 0.71 +/- 0.07 A for heavy atoms to the mean structure. No distance constraint was violated by more than 0.26 A in the structure family. Despite the low number of conserved residues shared with other PC homologues, the overall folding pattern of P. hollandica PC is similar to other PCs, in that the protein forms a two-sheet beta-barrel tertiary structure. The greatest variability among the backbone structures is seen in the loop region from residues 47-60. The differences seen in the P. hollandica PC homologue likely arise due to a small deletion of 2-4 residues compared to the PC consensus; this yields a less extended loop containing a short alpha-helix from residues Ala52-Leu55. Additionally, the protein has an altered hydrophobic patch thought to be important in binding reaction partners. Whereas the backbone structure is very similar within the loops of the hydrophobic region, the presence of two unique residues (Tyr12 and Pro14) yields a structurally different hydrophobic surface likely important in binding P. hollandica Photosystem I.


  • Organizational Affiliation

    Center for Photochemical Sciences, Department of Biological Sciences, Bowling Green State University, OH 43403, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (PLASTOCYANIN)97Prochlorothrix hollandicaMutation(s): 0 
Gene Names: PETE
EC: 1.10.99.1
Membrane Entity: Yes 
UniProt
Find proteins for P50057 (Prochlorothrix hollandica)
Explore P50057 
Go to UniProtKB:  P50057
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP50057
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
CU1
Query on CU1

Download Ideal Coordinates CCD File 
B [auth A]COPPER (I) ION
Cu
VMQMZMRVKUZKQL-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 40 
  • Conformers Submitted: 
  • Selection Criteria: LOWEST TARGET FUNCTION 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-04-27
    Type: Initial release
  • Version 1.1: 2007-10-16
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-02-16
    Changes: Data collection, Database references, Derived calculations
  • Version 1.4: 2023-12-27
    Changes: Data collection