PMID- 10048324
OWN - NLM
STAT- MEDLINE
DCOM- 19990506
LR  - 20181113
IS  - 0961-8368 (Print)
IS  - 1469-896X (Electronic)
IS  - 0961-8368 (Linking)
VI  - 8
IP  - 2
DP  - 1999 Feb
TI  - Comparison of the backbone dynamics of the apo- and holo-carboxy-terminal domain 
      of the biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA 
      carboxylase.
PG  - 307-17
AB  - The biotin carboxyl carrier protein (BCCP) is a subunit of acetyl-CoA 
      carboxylase, a biotin-dependent enzyme that catalyzes the first committed step of 
      fatty acid biosynthesis. In its functional cycle, this protein engages in 
      heterologous protein-protein interactions with three distinct partners, depending 
      on its state of post-translational modification. Apo-BCCP interacts specifically 
      with the biotin holoenzyme synthetase, BirA, which results in the 
      post-translational attachment of biotin to a single lysine residue on BCCP. 
      Holo-BCCP then interacts with the biotin carboxylase subunit of acetyl-CoA 
      carboxylase, which leads to the addition of the carboxylate group of bicarbonate 
      to biotin. Finally, the carboxy-biotinylated form of BCCP interacts with 
      transcarboxylase in the transfer of the carboxylate to acetyl-CoA to form 
      malonyl-CoA. The determinants of protein-protein interaction specificity in this 
      system are unknown. The NMR solution structure of the unbiotinylated form of an 
      87 residue C-terminal domain fragment (residue 70-156) of BCCP (holoBCCP87) and 
      the crystal structure of the biotinylated form of a C-terminal fragment (residue 
      77-156) of BCCP from Escherichia coli acetyl-CoA carboxylase have previously been 
      determined. Comparative analysis of these structures provided evidence for small, 
      localized conformational changes in the biotin-binding region upon biotinylation 
      of the protein. These structural changes may be important for regulating specific 
      protein-protein interactions. Since the dynamic properties of proteins are 
      correlated with local structural environments, we have determined the relaxation 
      parameters of the backbone 15N nuclear spins of holoBCCP87, and compared these 
      with the data obtained for the apo protein. The results indicate that upon 
      biotinylation, the inherent mobility of the biotin-binding region and the 
      protruding thumb, with which the biotin group interacts in the holo protein, are 
      significantly reduced.
FAU - Yao, X
AU  - Yao X
AD  - Department of Chemistry and Biochemistry, University of Maryland Baltimore 
      County, 21250, USA.
FAU - Soden, C Jr
AU  - Soden C Jr
FAU - Summers, M F
AU  - Summers MF
FAU - Beckett, D
AU  - Beckett D
LA  - eng
GR  - GM 46511/GM/NIGMS NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Protein Sci
JT  - Protein science : a publication of the Protein Society
JID - 9211750
RN  - 0 (Apoenzymes)
RN  - 0 (Carrier Proteins)
RN  - 0 (Holoenzymes)
RN  - EC 6.- (Fatty Acid Synthase, Type II)
RN  - EC 6.4.1.2 (Acetyl-CoA Carboxylase)
RN  - EC 6.4.1.2 (biotin carboxyl carrier protein)
SB  - IM
MH  - Acetyl-CoA Carboxylase/*chemistry
MH  - Apoenzymes/analysis
MH  - Biotinylation
MH  - Carrier Proteins/*chemistry
MH  - Computer Simulation
MH  - Crystallography, X-Ray
MH  - Escherichia coli/chemistry
MH  - Fatty Acid Synthase, Type II
MH  - Holoenzymes/analysis
MH  - Magnetic Resonance Spectroscopy
MH  - Protein Processing, Post-Translational
MH  - Protein Structure, Secondary
PMC - PMC2144255
EDAT- 1999/02/27 03:14
MHDA- 2001/03/28 10:01
PMCR- 1999/08/01
CRDT- 1999/02/27 03:14
PHST- 1999/02/27 03:14 [pubmed]
PHST- 2001/03/28 10:01 [medline]
PHST- 1999/02/27 03:14 [entrez]
PHST- 1999/08/01 00:00 [pmc-release]
AID - 10.1110/ps.8.2.307 [doi]
PST - ppublish
SO  - Protein Sci. 1999 Feb;8(2):307-17. doi: 10.1110/ps.8.2.307.