PMID- 11700068
OWN - NLM
STAT- MEDLINE
DCOM- 20011207
LR  - 20131121
IS  - 0022-2836 (Print)
IS  - 0022-2836 (Linking)
VI  - 313
IP  - 5
DP  - 2001 Nov 9
TI  - Crystal structure of the liganded SCP-2-like domain of human peroxisomal 
      multifunctional enzyme type 2 at 1.75 A resolution.
PG  - 1127-38
AB  - beta-Oxidation of amino acyl coenzyme A (acyl-CoA) species in mammalian 
      peroxisomes can occur via either multifunctional enzyme type 1 (MFE-1) or type 2 
      (MFE-2), both of which catalyze the hydration of trans-2-enoyl-CoA and the 
      dehydrogenation of 3-hydroxyacyl-CoA, but with opposite chiral specificity. MFE-2 
      has a modular organization of three domains. The function of the C-terminal 
      domain of the mammalian MFE-2, which shows similarity with sterol carrier protein 
      type 2 (SCP-2), is unclear. Here, the structure of the SCP-2-like domain 
      comprising amino acid residues 618-736 of human MFE-2 (d Delta h Delta SCP-2L) 
      was solved at 1.75 A resolution in complex with Triton X-100, an analog of a 
      lipid molecule. This is the first reported structure of an MFE-2 domain. The d 
      Delta h Delta SCP-2L has an alpha/beta-fold consisting of five beta-strands and 
      five alpha-helices; the overall architecture resembles the rabbit and human SCP-2 
      structures. However, the structure of d Delta h Delta SCP-2L shows a hydrophobic 
      tunnel that traverses the protein, which is occupied by an ordered Triton X-100 
      molecule. The tunnel is large enough to accommodate molecules such as 
      straight-chain and branched-chain fatty acyl-CoAs and bile acid intermediates. 
      Large empty apolar cavities are observed near the exit of the tunnel and between 
      the helices C and D. In addition, the C-terminal peroxisomal targeting signal is 
      ordered in the structure and solvent-exposed, which is not the case with 
      unliganded rabbit SCP-2, supporting the hypothesis of a ligand-assisted targeting 
      mechanism.
CI  - Copyright 2001 Academic Press.
FAU - Haapalainen, A M
AU  - Haapalainen AM
AD  - Biocenter Oulu and Department of Biochemistry, University of Oulu, FIN-90014, 
      Finland.
FAU - van Aalten, D M
AU  - van Aalten DM
FAU - Merilainen, G
AU  - Merilainen G
FAU - Jalonen, J E
AU  - Jalonen JE
FAU - Pirila, P
AU  - Pirila P
FAU - Wierenga, R K
AU  - Wierenga RK
FAU - Hiltunen, J K
AU  - Hiltunen JK
FAU - Glumoff, T
AU  - Glumoff T
LA  - eng
SI  - PDB/1IKT
PT  - Journal Article
PL  - Netherlands
TA  - J Mol Biol
JT  - Journal of molecular biology
JID - 2985088R
RN  - 0 (Carrier Proteins)
RN  - 0 (Ligands)
RN  - 0 (Multienzyme Complexes)
RN  - 0 (Plant Proteins)
RN  - 0 (sterol carrier proteins)
RN  - 9002-93-1 (Octoxynol)
RN  - EC 1.1.1.- (3-Hydroxyacyl CoA Dehydrogenases)
RN  - EC 4.2.1.17 (Enoyl-CoA Hydratase)
SB  - IM
MH  - 3-Hydroxyacyl CoA Dehydrogenases/*chemistry/*metabolism
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Carrier Proteins/*chemistry
MH  - Crystallography, X-Ray
MH  - Enoyl-CoA Hydratase/*chemistry/*metabolism
MH  - Humans
MH  - Ligands
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Multienzyme Complexes/*chemistry/*metabolism
MH  - Octoxynol/chemistry/*metabolism
MH  - *Plant Proteins
MH  - Protein Binding
MH  - Protein Structure, Secondary
MH  - Protein Structure, Tertiary
MH  - Sequence Alignment
MH  - Static Electricity
MH  - Structure-Activity Relationship
MH  - Surface Plasmon Resonance
EDAT- 2001/11/09 10:00
MHDA- 2002/01/05 10:01
CRDT- 2001/11/09 10:00
PHST- 2001/11/09 10:00 [pubmed]
PHST- 2002/01/05 10:01 [medline]
PHST- 2001/11/09 10:00 [entrez]
AID - S0022-2836(01)95084-3 [pii]
AID - 10.1006/jmbi.2001.5084 [doi]
PST - ppublish
SO  - J Mol Biol. 2001 Nov 9;313(5):1127-38. doi: 10.1006/jmbi.2001.5084.