1AV1

CRYSTAL STRUCTURE OF HUMAN APOLIPOPROTEIN A-I


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 4.00 Å
  • R-Value Free: 0.428 
  • R-Value Work: 0.382 
  • R-Value Observed: 0.382 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation.

Borhani, D.W.Rogers, D.P.Engler, J.A.Brouillette, C.G.

(1997) Proc Natl Acad Sci U S A 94: 12291-12296

  • DOI: https://doi.org/10.1073/pnas.94.23.12291
  • Primary Citation of Related Structures:  
    1AV1

  • PubMed Abstract: 

    The structure of truncated human apolipoprotein A-I (apo A-I), the major protein component of high density lipoprotein, has been determined at 4-A resolution. The crystals comprise residues 44-243 (exon 4) of apo A-I, a fragment that binds to lipid similarly to intact apo A-I and that retains the lipid-bound conformation even in the absence of lipid. The molecule consists almost entirely of a pseudo-continuous, amphipathic alpha-helix that is punctuated by kinks at regularly spaced proline residues; it adopts a shape similar to a horseshoe of dimensions 125 x 80 x 40 A. Four molecules in the asymmetric unit associate via their hydrophobic faces to form an antiparallel four-helix bundle with an elliptical ring shape. Based on this structure, we propose a model for the structure of apo A-I bound to high density lipoprotein.


  • Organizational Affiliation

    Department of Organic Chemistry, Southern Research Institute, Birmingham, AL 35205, USA. borhani@sri.org


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
APOLIPOPROTEIN A-I
A, B, C, D
201Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P02647 (Homo sapiens)
Explore P02647 
Go to UniProtKB:  P02647
PHAROS:  P02647
GTEx:  ENSG00000118137 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP02647
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 4.00 Å
  • R-Value Free: 0.428 
  • R-Value Work: 0.382 
  • R-Value Observed: 0.382 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 97.47α = 90
b = 113.87β = 90
c = 196.19γ = 90
Software Package:
Software NamePurpose
HASSPmodel building
X-PLORmodel building
X-PLORrefinement
MOSFLMdata reduction
CCP4data scaling
ROTAVATAdata scaling
TRUNCATEdata scaling
HASSPphasing
X-PLORphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-02-04
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-04-04
    Changes: Data collection, Other, Refinement description
  • Version 1.4: 2024-02-07
    Changes: Data collection, Database references