Structure of bovine lactoperoxidase with a partially linked heme moiety at 1.98 Å resolution

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• 作者：Prashant K. Singh ; Harsh V. Sirohi ; Naseer Iqbal ; Pragya Tiwari ; Punit Kaur ; Sujata Sharma ; Tej P. Singh ; ^{tpsingh.aiims@gmail.com}
• 关键词：Crystal structure ; Intermediate ; Stability ; Inhibition ; Distal heme side
• 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：1865
• 期：3
• 页码：329-335
• 全文大小：2211 K
• 卷排序：1865

文摘

In mature LPO, the heme moiety is linked to protein through two covalent bonds. In the present structure, the linkage involving Glu258 is observed in 50% molecules. In other 50% molecules, the side chain of Glu258 does not form covalent linkage. The side chain of unlinked Glu258 is located in the substrate binding site. The unlinked Glu258 blocks the substrate binding site.