2MKV

Structure of the NA,K-ATPASE regulatory protein FXYD2b in micelles


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 10 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Structure of the Na,K-ATPase regulatory protein FXYD2b in micelles: Implications for membrane-water interfacial arginines.

Gong, X.M.Ding, Y.Yu, J.Yao, Y.Marassi, F.M.

(2015) Biochim Biophys Acta 1848: 299-306

  • DOI: https://doi.org/10.1016/j.bbamem.2014.04.021
  • Primary Citation of Related Structures:  
    2MKV

  • PubMed Abstract: 

    FXYD2 is a membrane protein responsible for regulating the function of the Na,K-ATPase in mammalian kidney epithelial cells. Here we report the structure of FXYD2b, one of two splice variants of the protein, determined by NMR spectroscopy in detergent micelles. Solid-state NMR characterization of the protein embedded in phospholipid bilayers indicates that several arginine side chains may be involved in hydrogen bond interactions with the phospholipid polar head groups. The structure and the NMR data suggest that FXYD2b could regulate the Na,K-ATPase by modulating the effective membrane surface electrostatics near the ion binding sites of the pump.


  • Organizational Affiliation

    Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Sodium/potassium-transporting ATPase subunit gamma64Homo sapiensMutation(s): 2 
Gene Names: ATP1CATP1G1FXYD2FXYD2b
Membrane Entity: Yes 
UniProt & NIH Common Fund Data Resources
Find proteins for P54710 (Homo sapiens)
Explore P54710 
Go to UniProtKB:  P54710
PHAROS:  P54710
GTEx:  ENSG00000137731 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP54710
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 10 
  • Selection Criteria: structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-05-14
    Type: Initial release
  • Version 1.1: 2014-05-21
    Changes: Database references
  • Version 1.2: 2014-12-24
    Changes: Database references
  • Version 1.3: 2023-06-14
    Changes: Data collection, Database references, Other
  • Version 1.4: 2024-05-15
    Changes: Data collection, Database references