嗜热栖热菌HB8中一种新型金属β-内酰胺酶超家族蛋白TTHA1623的结构
Structure of TTHA1623, a novel metallo-beta-lactamase superfamily protein from Thermus thermophilus HB8.
作者信息
Yamamura Akihiro, Okada Akitoshi, Kameda Yasuhiro, Ohtsuka Jun, Nakagawa Noriko, Ebihara Akio, Nagata Koji, Tanokura Masaru
机构信息
Department of Applied Biological Chemistry, University of Tokyo, Yayoi, Bunkyo-ku, Japan.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 May 1;65(Pt 5):455-9. doi: 10.1107/S174430910901361X. Epub 2009 Apr 24.
Abstract
TTHA1623 is a metallo-beta-lactamase superfamily protein from the extremely thermophilic bacterium Thermus thermophilus HB8. Homologues of TTHA1623 exist in a wide range of bacteria and archaea and one eukaryote, Giardia lamblia, but their function remains unknown. To analyze the structural properties of TTHA1623, the crystal structures of its iron-bound and zinc-bound forms have been determined to 2.8 and 2.2 A resolution, respectively. TTHA1623 possesses an alphabetabetaalpha-fold similar to that of other metallo-beta-lactamase superfamily proteins with glyoxalase II-type metal coordination. However, TTHA1623 exhibits a putative substrate-binding pocket with a unique shape.
摘要
TTHA1623是一种来自嗜热栖热菌HB8的金属β-内酰胺酶超家族蛋白。TTHA1623的同源物存在于多种细菌、古菌以及一种真核生物——蓝氏贾第鞭毛虫中，但其功能仍不清楚。为了分析TTHA1623的结构特性，已分别确定了其铁结合形式和锌结合形式的晶体结构，分辨率分别为2.8 Å和2.2 Å。TTHA1623具有与其他具有乙二醛酶II型金属配位的金属β-内酰胺酶超家族蛋白相似的αβα折叠结构。然而，TTHA1623展现出一个形状独特的假定底物结合口袋。
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