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Maria C. Bewley
Brookhaven National Laboratory
From: 1/28/97 -8/25/03
Currently at:
Penn State
Past BNL Research Interests
My laboratory is interested in structure/function analysis of multicomponent enzymatic pathways.
Our understanding of the function of such pathways is often incomplete because typically individual
proteins have been studied in isolation rather than in the context of a biologically relevant
complex. There are two systems that I am focusing on; the primary system is the pathway by which
DNA double strand break (DSB) repair occurs in mammalian cells and the secondary system is the
electron transfer pathway of fatty acid biosynthesis. DSB repair is crucial to the survival of a
cell, yet its mechanism is relatively poorly understood. It is known that protein:protein
interactions play a crucial part in the regulation and action of repair, and some of the players
are already known including DNA protein kinase (DNA-PK), Ku70:80, XRCC4 and DNA ligase IV.
Fatty acid desaturation occurs in all mammals and involves the transfer of electrons from b5
reductase(B5R)-bound NADH to cytochrome b5. How this transfer is achieved is one of the key
unanswered questions in this pathway. My research centers on obtaining their structures, alone,
and in biologically relevant complexes.
Select Past Publications
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MacGillivray R.T.A., Bewley M.C., Smith C.A., He Q.Y., Mason A.B., Woodworth R.C. and Baker E.N.
Mutation of the iron ligand His249 to Glu in the N-lobe of human transferrin
abolishes the dilysine 'trigger' but does not significantly affect iron release.
Biochem., 39:1211-1216 (2000).
PubMed
PDB file 1DTG
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Bewley M.C., Springer K., Zhang Y.-B., Freimuth P., and Flanagan J.M.
Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR.
Science, 286:1579-1583 (1999).
Full Text (pdf)
PubMed
PDB files
1KAC,
1NOB
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Bewley M.C., Jeffrey P.D., Patchett M.L., Kanyo Z.F., and Baker E.N.
Crystal structures of Bacillus caldovelox arginase in complex with substrate and inhibitors
reveal new insights into activation, inhibition and catalysisin the arginase superfamily.
Structure, 7:435-448 (1999).
PubMed PDB files 1CEV,
2CEV,
3CEV,
4CEV,
5CEV
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Bewley M.C., Tam B.M., Grewal J., He S., Shewry S., Murphy M.E.,
Mason A.B., Woodworth R.C., Baker E.N., and MacGillivray R.T.
X-ray crystallography and mass spectroscopy reveal that the N-lobe of human
transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.
Biochemistry, 38:2535-2541 (1999).
PubMed
PDB file 1B3E
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Freimuth P., Springer K., Berard C., Hainfeld J., Bewley M., and Flanagan J.
Coxsackievirus and adenovirus receptor amino-terminal immunoglobulin V
related domain binds adenovirus type 2 and fiber knob from adenovirus type 12.
J. Virol., 73:1392-1398 (1999).
Full Text (pdf)
PubMed
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Qin B.Y., Bewley M.C., Creamer L.K., Baker E.N., and Jameson G.B.
Functional implications of structural differences between variants A and B
of bovine beta-lactoglobulin.
Protein Sci., 8:75-83 (1999).
PubMed
PDB file 1BSQ
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Qin B.Y., Bewley M.C., Creamer L.K., Baker H.M., Baker E.N., and Jameson G.B.
Structural basis of the Tanford transition of bovine beta-lactoglobulin.
Biochemistry, 37:14014-14023 (1998).
PubMed
PDB files 1BSY,
2BLG,
3BLG
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Jeffrey P.D., Bewley M.C., MacGillivray R.T., Mason A., Woodworth R., and Baker E.N.
Ligand-induced conformational change in transferrins: crystal structure of
the open form of the N-terminal half-molecule of human transferrin.
Biochemistry, 37:13978-13986 (1998).
PubMed
PDB files 1BP5,
1BTJ
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Bewley M.C., Qin B.Y., Jameson G.B., Sawyer L., and Baker E.N.
Bovine P-lactoglobulin and its variants: A three dimensional perspective.
In: Milk Protein Polymorphism, Int. Fed. Bull. Special Issue.
IDF: Brussels, pp. 101-109 (1998).
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MacGillivray R.T., Moore S.A., Chen J., Anderson B.F., Baker H.,
Luo Y., Bewley M., Smith C.A., Murphy M.E., Wang Y., Mason A.B.,
Woodworth R.C., Brayer G.D., and Baker E.N.
Two high-resolution crystal structures of the recombinant N-lobe of human
transferrin reveal a structural change implicated in iron release.
Biochemistry, 37:7919-7928 (1998). PDB files 1A8F,
1A8E
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Attwood T.K., Avison H., Beck M.E., Bewley M., Bleasby A.J.,
Brewster F., Cooper P., Degtyarenko K., Geddes A.J., Flower D.R.,
Kelly M.P., Lott S., Measures K.M., Parry-Smith D.J., Perkins D.N.,
Scordis P., Scott D., and Worledge C.
The PRINTS database of protein fingerprints: A novel information resource
for computational molecular biology.
J. Chem. Inf. Comput. Sci., 37:417-424 (1997).
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Bewley M.C., Lot, J.S., Baker E.N., and Patchett M.L.
The cloning, expression, and crystallization of a thermostable arginase.
FEBS Letts., 386:215-218 (1996).
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Holzenberg A., Bewley M.C., Wilson F.H., Nicholson W.V., and Ford R.C.
Three dimensional structure of photosystem II.
Nature, 363:470-472 (1993).
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Bewley M.C., Boustead C.M., Walker J.H., Waller D.A., and Huber R.
Structure of chicken annexin V at 2.25 A resolution.
Biochemistry, 32:3923-3929 (1993).
PDB file 1ALA
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Walker J.H., Boustead C.M., Koster J.J., Bewley M., and Waller D.A.
Annexin V, a calcium dependent phospholipid-binding protein.
Biochem. Soc. Trans., 20:828-833 (1992).
Last Modified: April 10, 2009
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