Structure of the SHV-1 -Lactamase
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- 作者：Alexandre P. Kuzin ; Michiyoshi Nukaga ; Yasuko Nukaga ; Andrea M. Hujer ; Robert A. Bonomo ; and James R. Knox
- 刊名：Biochemistry
- 出版年：1999
- 出版时间：May 4, 1999
- 年：1999
- 卷：38
- 期：18
- 页码：5720 - 5727
- 全文大小：308K
- 年卷期：v.38,no.18(May 4, 1999)
- ISSN：1520-4995
文摘
The X-ray crystallographic structure of the SHV-1 
-lactamase has been established. The enzymecrystallizes from poly(ethylene glycol) at pH 7 in space group P212121 with cell dimensions a = 49.6 Å,b = 55.6 Å, and c = 87.0 Å. The structure was solved by the molecular replacement method, and themodel has been refined to an R-factor of 0.18 for all data in the range 8.0-1.98 Å resolution. Deviationsof model bonds and angles from ideal values are 0.018 Å and 1.8
, respectively. Overlay of all 263
pha.gif" BORDER=0>-carbon atoms in the SHV-1 and TEM-1 -lactamases results in an rms deviation of 1.4 Å. Largestdeviations occur in the H10 helix (residues 218-224) and in the loops between strands in the -sheet. Allatoms in residues 70, 73, 130, 132, 166, and 234 in the catalytic site of SHV-1 deviate only 0.23 Å (rms)from atoms in TEM-1. However, the width of the substrate binding cavity in SHV-1, as measured fromthe 104-105 and 130-132 loops on one side to the 235-238 -strand on the other side, is 0.7-1.2 Åwider than in TEM-1. A structural analysis of the highly different affinity of SHV-1 and TEM-1 for the-lactamase inhibitory protein BLIP focuses on interactions involving Asp/Glu104.
-lactamase has been established. The enzymecrystallizes from poly(ethylene glycol) at pH 7 in space group P212121 with cell dimensions a = 49.6 Å,b = 55.6 Å, and c = 87.0 Å. The structure was solved by the molecular replacement method, and themodel has been refined to an R-factor of 0.18 for all data in the range 8.0-1.98 Å resolution. Deviationsof model bonds and angles from ideal values are 0.018 Å and 1.8, respectively. Overlay of all 263pha.gif" BORDER=0>-carbon atoms in the SHV-1 and TEM-1 -lactamases results in an rms deviation of 1.4 Å. Largestdeviations occur in the H10 helix (residues 218-224) and in the loops between strands in the -sheet. Allatoms in residues 70, 73, 130, 132, 166, and 234 in the catalytic site of SHV-1 deviate only 0.23 Å (rms)from atoms in TEM-1. However, the width of the substrate binding cavity in SHV-1, as measured fromthe 104-105 and 130-132 loops on one side to the 235-238 -strand on the other side, is 0.7-1.2 Åwider than in TEM-1. A structural analysis of the highly different affinity of SHV-1 and TEM-1 for the-lactamase inhibitory protein BLIP focuses on interactions involving Asp/Glu104.