PMID- 10089347
OWN - NLM
STAT- MEDLINE
DCOM- 19990415
LR  - 20190516
IS  - 0907-4449 (Print)
IS  - 0907-4449 (Linking)
VI  - 55
IP  - Pt 2
DP  - 1999 Feb
TI  - Structure of recombinant human lactoferrin expressed in Aspergillus awamori.
PG  - 403-7
AB  - Human lactoferrin (hLf) has considerable potential as a therapeutic agent.
      Overexpression of hLf in the fungus Aspergillus awamori has resulted in the
      availability of very large quantities of this protein. Here, the
      three-dimensional structure of the recombinant hLf has been determined by X-ray
      crystallography at a resolution of 2.2 A. The final model, comprising 5339
      protein atoms (residues 1-691, 294 solvent molecules, two Fe3+and two CO32-
      ions), gives an R factor of 0.181 (free R = 0.274) after refinement against 32231
      reflections in the resolution range 10-2.2 A. Superposition of the recombinant
      hLf structure onto the native milk hLf structure shows a very high level of
      correspondence; the main-chain atoms for the entire polypeptide can be
      superimposed with an r.m.s. deviation of only 0.3 A and there are no significant 
      differences in side-chain conformations or in the iron-binding sites. Dynamic
      properties, as measured by B-value distributions or iron-release kinetics, also
      agree closely. This shows that the structure of the protein is not affected by
      the mode of expression, the use of strain-improvement procedures or the changes
      in glycosylation due to the fungal system.
FAU - Sun, X L
AU  - Sun XL
AD  - Departments of Biochemistry and Chemistry, Massey University, Palmerston North,
      New Zealand.
FAU - Baker, H M
AU  - Baker HM
FAU - Shewry, S C
AU  - Shewry SC
FAU - Jameson, G B
AU  - Jameson GB
FAU - Baker, E N
AU  - Baker EN
LA  - eng
SI  - PDB/1BOL
GR  - HD-20859/HD/NICHD NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Acta Crystallogr D Biol Crystallogr
JT  - Acta crystallographica. Section D, Biological crystallography
JID - 9305878
RN  - 0 (Recombinant Proteins)
RN  - EC 3.4.21.- (Lactoferrin)
SB  - IM
MH  - Aspergillus/*genetics
MH  - Crystallography, X-Ray
MH  - Glycosylation
MH  - Humans
MH  - Lactoferrin/*chemistry
MH  - Models, Molecular
MH  - Protein Conformation
MH  - Recombinant Proteins/chemistry
EDAT- 1999/03/25 03:01
MHDA- 2000/06/23 11:00
CRDT- 1999/03/25 03:01
PHST- 1999/03/25 03:01 [pubmed]
PHST- 2000/06/23 11:00 [medline]
PHST- 1999/03/25 03:01 [entrez]
AID - LI0292 [pii]
AID - 10.1107/s0907444998011226 [doi]
PST - ppublish
SO  - Acta Crystallogr D Biol Crystallogr. 1999 Feb;55(Pt 2):403-7. doi:
      10.1107/s0907444998011226.