X-ray crystallographic studies on Particulate Methane Monooxygenase, Thioredoxin A and Arginine Decarboxylase

The work presented in this thesis describes the X-ray crystallographic studies of particulatemethane monoxygenase (pMMO) from Methylococcus capsulatus (Bath), thioredoxin A(BsTrxA) from Bacillus subtilis and arginine decarboxylase (AdiA) from Escherichia coli.1. pMMO is a respiratory enzyme that cat...

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Main Author: Andrell, Juni
Other Authors: Carpenter, Liz ; Iwata, So
Published: Imperial College London 2008
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Online Access:http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.506400
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spelling ndltd-bl.uk-oai-ethos.bl.uk-5064002017-08-30T03:15:52ZX-ray crystallographic studies on Particulate Methane Monooxygenase, Thioredoxin A and Arginine DecarboxylaseAndrell, JuniCarpenter, Liz ; Iwata, So2008The work presented in this thesis describes the X-ray crystallographic studies of particulatemethane monoxygenase (pMMO) from Methylococcus capsulatus (Bath), thioredoxin A(BsTrxA) from Bacillus subtilis and arginine decarboxylase (AdiA) from Escherichia coli.1. pMMO is a respiratory enzyme that catalyses the first step in the metabolic pathway inmethanotrophic bacteria by converting methane to methanol. The crystal structure of thisintegral membrane protein was determined by molecular replacement to 3.5 ? resolution. The three metal sites in pMMO were confirmed to be a mononuclear copper site, adinuclear copper site and a mononuclear zinc site.2. Thioredoxin is a ubiquitous protein present in nearly all known organisms. Its purposein the cell is to maintain cysteine-containing proteins in the reduced state by convertingintramolecular disulfide bonds to dithiols in a redox reaction. The crystal structure of anactive site mutant of BsTrxA was determined by molecular replacement to 1.5 ?resolution. The structure shows a homodimer that resembles enzyme-substrate reactionintermediates.3. AdiA is a vitamin B6-dependent enzyme that catalyses the decarboxylation of arginineinto agmatine. It forms a part of an enzymatic system in E. coli that contribute to makingthis organism acid resistant. The structure of arginine decarboxylase (AdiA) from E. coliwas determined by multiple isomorphous replacement and anomalous scattering (MIRAS)methods to 2.4 ? resolution. The structure revealed a ~800 kDa decamer composed as apentamer of five homodimers. AdiA becomes active as the cellular environment becomesmore acidic. The structure of AdiA suggests how functional decamers associate withdecreasing pH or disassociates into inactive homodimers with increasing pH. The enzymemechanism and determinants for substrate specificity are discussed within the frameworkof the structure and comparisons with related structures are made.571.4Imperial College Londonhttp://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.506400http://hdl.handle.net/10044/1/4634Electronic Thesis or Dissertation
collection NDLTD
sources NDLTD
topic 571.4
spellingShingle 571.4
Andrell, Juni
X-ray crystallographic studies on Particulate Methane Monooxygenase, Thioredoxin A and Arginine Decarboxylase
description The work presented in this thesis describes the X-ray crystallographic studies of particulatemethane monoxygenase (pMMO) from Methylococcus capsulatus (Bath), thioredoxin A(BsTrxA) from Bacillus subtilis and arginine decarboxylase (AdiA) from Escherichia coli.1. pMMO is a respiratory enzyme that catalyses the first step in the metabolic pathway inmethanotrophic bacteria by converting methane to methanol. The crystal structure of thisintegral membrane protein was determined by molecular replacement to 3.5 ? resolution. The three metal sites in pMMO were confirmed to be a mononuclear copper site, adinuclear copper site and a mononuclear zinc site.2. Thioredoxin is a ubiquitous protein present in nearly all known organisms. Its purposein the cell is to maintain cysteine-containing proteins in the reduced state by convertingintramolecular disulfide bonds to dithiols in a redox reaction. The crystal structure of anactive site mutant of BsTrxA was determined by molecular replacement to 1.5 ?resolution. The structure shows a homodimer that resembles enzyme-substrate reactionintermediates.3. AdiA is a vitamin B6-dependent enzyme that catalyses the decarboxylation of arginineinto agmatine. It forms a part of an enzymatic system in E. coli that contribute to makingthis organism acid resistant. The structure of arginine decarboxylase (AdiA) from E. coliwas determined by multiple isomorphous replacement and anomalous scattering (MIRAS)methods to 2.4 ? resolution. The structure revealed a ~800 kDa decamer composed as apentamer of five homodimers. AdiA becomes active as the cellular environment becomesmore acidic. The structure of AdiA suggests how functional decamers associate withdecreasing pH or disassociates into inactive homodimers with increasing pH. The enzymemechanism and determinants for substrate specificity are discussed within the frameworkof the structure and comparisons with related structures are made.
author2 Carpenter, Liz ; Iwata, So
author_facet Carpenter, Liz ; Iwata, So
Andrell, Juni
author Andrell, Juni
author_sort Andrell, Juni
title X-ray crystallographic studies on Particulate Methane Monooxygenase, Thioredoxin A and Arginine Decarboxylase
title_short X-ray crystallographic studies on Particulate Methane Monooxygenase, Thioredoxin A and Arginine Decarboxylase
title_full X-ray crystallographic studies on Particulate Methane Monooxygenase, Thioredoxin A and Arginine Decarboxylase
title_fullStr X-ray crystallographic studies on Particulate Methane Monooxygenase, Thioredoxin A and Arginine Decarboxylase
title_full_unstemmed X-ray crystallographic studies on Particulate Methane Monooxygenase, Thioredoxin A and Arginine Decarboxylase
title_sort x-ray crystallographic studies on particulate methane monooxygenase, thioredoxin a and arginine decarboxylase
publisher Imperial College London
publishDate 2008
url http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.506400
work_keys_str_mv AT andrelljuni xraycrystallographicstudiesonparticulatemethanemonooxygenasethioredoxinaandargininedecarboxylase
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