Purification, crystallization, and X-ray crystallographic analysis of CALA-like lipase 7 from Cordyceps militaris

• 발행기관: 한국구조생물학회
• 저자명: Han-Gyeol Woo Juno Lee Eun-Kyung Yoon Pahn-Shick Chang Jeong-Sun Kim
• 간행물 정보: 『Biodesign』Vol 13, No 2, Jun, 17~21쪽, 전체 5쪽
• 주제분류: 자연과학 > 생물학
• 파일형태: PDF
• 발행일자: 2025.06.30

국문 초록

Candida antarctica lipase A (CALA) is a triacylglycerol hydrolase that reversibly hydrolyzes sn-2 ester bond. The CALAlike superfamily is classified based on several distinctive structural and functional features. CALA-like Cordyceps militaris lipase 7 (CACML7) exhibits a slightly different substrate preference, compared with CALA. To provide a structural basis for its substrate specificity, the CACML7 encoding gene was cloned into the pPICZα A vector, and expressed in Pichia pastoris X-33. The purified CACML7 protein was crystallized using a precipitant solution composed of 0.10 M citric acid (pH 3.5) and 2.15 M ammonium sulfate. Diffraction data were collected at 1.80 Å resolution. The crystal belonged to the orthorhombic space group I222 with unit-cell parameters a = 65.57 Å, b = 127.03 Å, c = 141.11 Å, and α = β = γ = 90°. The initial position of the one protein molecule in the asymmetric unit was determined by molecular replacement.

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INTRODUCTION

RESULTS AND DISCUSSION

METHODS

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