A.P. Kuzin

New York Structural Biology Center

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G.T. Montelione

Rensselaer Polytechnic Institute

J.F. Hunt

Columbia University

T.B. Acton

Ollscoil na Gaillimhe – University of Galway

J. Seetharaman

St. Jude Children's Research Hospital

Rong Xiao

Huazhong Agricultural University

S.M. Vorobiev

Rutgers, The State University of New Jersey

K. Cunningham

Vanderbilt University

M.C. Baran

AGH University of Krakow

J.K. Everett

University of Pennsylvania

M. Abashidze

New York Structural Biology Center

Cooperative Institutions

Rutgers, The State University of New Jersey

Joint Center for Structural Genomics

Structural Genomics Consortium

Columbia University

Howard Hughes Medical Institute

University of Washington

New York Structural Biology Center

Johnson University

University of Connecticut

Chinese Academy of Sciences

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CEFOTAXIME COMPLEXED WITH THE STREPTOMYCES R61 DD-PEPTIDASE

James R. Knox A.P. Kuzin

10.2210/pdb1cef/pdb

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Citations (2)

The Structure of Vimentin Linker 1 and Rod 1B Domains Characterized by Site-directed Spin-labeling Electron Paramagnetic Resonance (SDSL-EPR) and X-ray Crystallography

Journal of Biological Chemistry (2012)

Atya Aziz John F. Hess Madhu S. Budamagunta John C. Voss A.P. Kuzin

Site-directed spin labeling

Tetramer

Sequence (biology)

Oligomer

Pulsed EPR

Trimer

10.1074/jbc.m111.334011

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Citations (57)

Crystal structure of putative transcriptional regulator ywtF from Bacillus subtilis, Northeast Structural Genomics Consortium Target SR736

A.P. Kuzin M. Su J. Seetharaman M. Mao R. Xiao

Structural genomics

10.2210/pdb3mej/pdb

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X-Ray Crystal Structure of the Metal-containing Protein AF0104 from Archaeoglobus fulgidus. Northeast Structural Genomics Consortium Target GR103.

A.P. Kuzin M. Abashidze Yitong Fang C. Chen K. Cunningham

Structural genomics

Structural Biology

10.2210/pdb2h6l/pdb

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Purification and crystallographic studies of aD-alanyl-D-alanine carboxypeptidase fromB. stearothermophilus

Acta Crystallographica Section A Foundations of Crystallography (1996)

A.P. Kuzin J. L. Frost S. L. Condron Julia Kelly

D-alanyl-D-alanine carboxypeptidases (Cpases) m•e involved in bacterial cell wall biosynthesis and are targets of ~-lactam antibiotics.The gene for a Cpase from B. stearothermo!plzilus has been modified by R. Manning and C. Despreaux ofHoffmann-LaRoche to remove a 26-residue C terminal fragment thafm1chors the enzyme in the bacterial membrane.The engineered gene was inserted in Pichia pastoris, and the soluble 43kDa enzyme wasexcreted into the medium.Ammonium sulfate precipitation and Fast Protein Liquid Chromatography using a Mono-S (cationic) column were used to purify the enzyme.The enzyme can also be solubilized via trypsin or chymotrypsin digestion.Cpase was crystallized from 20nLlVI Tris buffer, pH 7.5, with 0.2M NaCl and 10% PEG 8000 in P2 1 2 1 2 (a=85.1A.b=l40.3A,c=l67.3A).There m•e at least four molecules in the asymmetric unit cell.Native data to 3.2A and data for a K2PtCL; derivative have been collected.The sequence of Cpase was compared to that of the DD-transpeptidase from Streptomyces Kl5 (Englebert, S. eta! .. 1994, 1. Mol.Bioi.

Carboxypeptidase A

Alanine

10.1107/s0108767396094809

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Three-dimensional structure of the protein prib from ralstonia solanacearum at the resolution 1.8a. northeast structural genomics consortium target rsr213c

A.P. Kuzin H. Neely J. Seetharaman H. Wang S. Sahdev

Ralstonia solanacearum

Structural genomics

10.2210/pdb4fdb/pdb

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