Petsko GA - Search Results

1

X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica.

Munih P, Moulin A, Stamper CC, Bennett B, Ringe D, Petsko GA, Holz RC. Munih P, et al. Among authors: petsko ga. J Inorg Biochem. 2007 Aug;101(8):1099-107. doi: 10.1016/j.jinorgbio.2007.03.010. Epub 2007 Apr 11. J Inorg Biochem. 2007. PMID: 17574677

2

The 1.20 A resolution crystal structure of the aminopeptidase from Aeromonas proteolytica complexed with tris: a tale of buffer inhibition.

Desmarais WT, Bienvenue DL, Bzymek KP, Holz RC, Petsko GA, Ringe D. Desmarais WT, et al. Among authors: petsko ga. Structure. 2002 Aug;10(8):1063-72. doi: 10.1016/s0969-2126(02)00810-9. Structure. 2002. PMID: 12176384 Free article.

3

Xylose isomerase in substrate and inhibitor michaelis states: atomic resolution studies of a metal-mediated hydride shift.

Fenn TD, Ringe D, Petsko GA. Fenn TD, et al. Among authors: petsko ga. Biochemistry. 2004 Jun 1;43(21):6464-74. doi: 10.1021/bi049812o. Biochemistry. 2004. PMID: 15157080

4

Spectroscopic and X-ray crystallographic characterization of bestatin bound to the aminopeptidase from Aeromonas (Vibrio) proteolytica.

Stamper CC, Bienvenue DL, Bennett B, Ringe D, Petsko GA, Holz RC. Stamper CC, et al. Among authors: petsko ga. Biochemistry. 2004 Aug 3;43(30):9620-8. doi: 10.1021/bi049126p. Biochemistry. 2004. PMID: 15274616

5

Kinetic, spectroscopic, and X-ray crystallographic characterization of the functional E151H aminopeptidase from Aeromonas proteolytica.

Bzymek KP, Moulin A, Swierczek SI, Ringe D, Petsko GA, Bennett B, Holz RC. Bzymek KP, et al. Among authors: petsko ga. Biochemistry. 2005 Sep 13;44(36):12030-40. doi: 10.1021/bi0505823. Biochemistry. 2005. PMID: 16142900

6

The high-resolution structures of the neutral and the low pH crystals of aminopeptidase from Aeromonas proteolytica.

Desmarais W, Bienvenue DL, Bzymek KP, Petsko GA, Ringe D, Holz RC. Desmarais W, et al. Among authors: petsko ga. J Biol Inorg Chem. 2006 Jun;11(4):398-408. doi: 10.1007/s00775-006-0093-x. Epub 2006 Apr 5. J Biol Inorg Chem. 2006. PMID: 16596389

7

Zinc coordination geometry and ligand binding affinity: the structural and kinetic analysis of the second-shell serine 228 residue and the methionine 180 residue of the aminopeptidase from Vibrio proteolyticus.

Ataie NJ, Hoang QQ, Zahniser MP, Tu Y, Milne A, Petsko GA, Ringe D. Ataie NJ, et al. Among authors: petsko ga. Biochemistry. 2008 Jul 22;47(29):7673-83. doi: 10.1021/bi702188e. Epub 2008 Jun 25. Biochemistry. 2008. PMID: 18576673 Free PMC article.

8

Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures.

Liu D, Momb J, Thomas PW, Moulin A, Petsko GA, Fast W, Ringe D. Liu D, et al. Among authors: petsko ga. Biochemistry. 2008 Jul 22;47(29):7706-14. doi: 10.1021/bi800368y. Biochemistry. 2008. PMID: 18627129 Free PMC article.

9

Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis.

Stamper C, Bennett B, Edwards T, Holz RC, Ringe D, Petsko G. Stamper C, et al. Biochemistry. 2001 Jun 19;40(24):7035-46. doi: 10.1021/bi0100891. Biochemistry. 2001. PMID: 11401547

10

Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution.

Shaw JP, Petsko GA, Ringe D. Shaw JP, et al. Among authors: petsko ga. Biochemistry. 1997 Feb 11;36(6):1329-42. doi: 10.1021/bi961856c. Biochemistry. 1997. PMID: 9063881

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