Phase determination of a homogentisate dioxygenase from Comamonas sp. strain P19

• 발행기관: 한국구조생물학회
• 저자명: Suk-Youl Park Byoung Yul Soh Jong-Chan Chae Jeong-Sun Kim
• 간행물 정보: 『Biodesign』Vol 5, No 3, Sep, 107~109쪽, 전체 3쪽
• 주제분류: 자연과학 > 생물학
• 파일형태: PDF
• 발행일자: 2017.09.30

영문 초록

In Comamonas sp. strain P19, homogentisate 1,2-dioxygenase (HGO) catalyzes the conversion of homogentisate to 4-maleylacetoacetate by aromatic ring scission, in the breakdown of tyrosine and phenylalanine. To determine the molecular background of the enzymatic mechanism of HGO in this zinc-resistant organism, hmgA encoding HGO of Comamonas sp. strain P19 was cloned, and the expressed protein was purified. The protein was crystallized in solutions I [25% (w/v) polyethylene glycol 3350 and 0.1 M trisodium citrate at pH 5.6] and II [1.4 M ammonium tartrate and 0.1 M bisTris at pH 5.5]. X-ray diffraction data were collected to 1.8 Å resolution using synchrotron radiation. The crystal belongs to the orthorhombic space group P2 1 2 1 2 1 , with unit cell dimensions of a = 73.2 Å, b = 100.0 Å, and c = 134.9 Å. A traceable electron density map was calculated using anomalous diffraction data obtained from a crystal soaked in zinc ions.

목차

INTRODUCTION

RESULTS AND DISCUSSION