Evidence of a Double-Lid Movement in Pseudomonas aeruginosa Lipase Insights from Molecular Dynamics Simulations 英文参考文献.docVIP

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Evidence of a Double-Lid Movement in Pseudomonas aeruginosa Lipase Insights from Molecular Dynamics Simulations 英文参考文献.doc

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Evidence of a Double-Lid Movement in Pseudomonas aeruginosa Lipase Insights from Molecular Dynamics Simulations 英文参考文献

EvidenceofaDouble-LidMovement inPseudomonasaeruginosaLipase: InsightsfromMolecularDynamicsSimulations Subbulakshmi Latha Cherukuvada1[,Aswin Sai Narain Seshasayee1[,Krishnan Raghunathan1[,Sharmila Anishetty1, Gautam Pennathur1,2* 1CentreforBiotechnology,AnnaUniversity,Chennai,India,2AU-KBCResearchCentre,MadrasInstituteofTechnology,Chennai,India Pseudomonas aeruginosa lipase is a 29-kDa protein that, following the determination of its crystal structure, was postulated to have a lid that stretched between residues 125 and 148. In this paper, using molecular dynamics simulations,weproposethatthereexists,inadditiontotheabove-mentionedlid,anovelsecondlidinthislipase.We furthershowthatthesecondlid,coveringresidues210–222,actsasatriggeringlidforthemovementofthefirst.We also investigate the role of hydrophobicity in the movement of the lids and show that two residues, Phe214 and Ala217,playimportantrolesinlidmovement.Toourknowledge,thisisthefirsttimethatadouble-lidmovementof thetypedescribedinourmanuscripthasbeenpresentedtothescientificcommunity.Thisworkalsoelucidatesthe interplayofhydrophobicinteractionsinthedynamics,andhencethefunction,ofanenzyme. Citation:CherukuvadaSL,SeshasayeeASN,RaghunathanK,AnishettyS,PennathurG(2005)Evidenceofadouble-lidmovementinPseudomonasaeruginosalipase:Insights frommoleculardynamicssimulations.PLoSCompBiol1(3):e28. Molecular dynamics (MD) studies have been used exten- sivelyinthestudyofproteinfolding[16]andenzymecatalysis Introduction Lipases are enzymes that catalyze both theformation and cleavage of long-chain acylglycerols [1]. In recent years, crystal structures of several lipases—bacterial, fungal and mammalian—have been determined [2–8]. Industrially, li- pases—especially those of bacterial and fungal origins—are seemingly attractive as biocatalysts due to their cofactor independence,broadsubstratespeci?city,enantioselectivity, and stability in organic solvents [9]. In addition, there have beenanumberofreportsimplicatinglipasesinpathoge