Umeå universitets logga

umu.sePublikationer
Ändra sökning
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Structural basis for thermophilic protein stability: structures of thermophilic and mesophilic malate dehydrogenases.
Umeå universitet, Teknisk-naturvetenskaplig fakultet, Umeå centrum för molekylär patogenes (UCMP) (Teknisk-naturvetenskaplig fakultet).
Visa övriga samt affilieringar
2002 (Engelska)Ingår i: J Mol Biol, ISSN 0022-2836, Vol. 318, nr 3, s. 707-21Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

The three-dimensional structure of four malate dehydrogenases (MDH) from thermophilic and mesophilic phototropic bacteria have been determined by X-ray crystallography and the corresponding structures compared. In contrast to the dimeric quaternary structure of most MDHs, these MDHs are tetramers and are structurally related to tetrameric malate dehydrogenases from Archaea and to lactate dehydrogenases. The tetramers are dimers of dimers, where the structures of each subunit and the dimers are similar to the dimeric malate dehydrogenases. The difference in optimal growth temperature of the corresponding organisms is relatively small, ranging from 32 to 55 degrees C. Nevertheless, on the basis of the four crystal structures, a number of factors that are likely to contribute to the relative thermostability in the present series have been identified. It appears from the results obtained, that the difference in thermostability between MDH from the mesophilic Chlorobium vibrioforme on one hand and from the moderate thermophile Chlorobium tepidum on the other hand is mainly due to the presence of polar residues that form additional hydrogen bonds within each subunit. Furthermore, for the even more thermostable Chloroflexus aurantiacus MDH, the use of charged residues to form additional ionic interactions across the dimer-dimer interface is favored. This enzyme has a favorable intercalation of His-Trp as well as additional aromatic contacts at the monomer-monomer interface in each dimer. A structural alignment of tetrameric and dimeric prokaryotic MDHs reveal that structural elements that differ among dimeric and tetrameric MDHs are located in a few loop regions. (c) 2002 Elsevier Science Ltd.

Ort, förlag, år, upplaga, sidor
2002. Vol. 318, nr 3, s. 707-21
Nyckelord [en]
Amino Acid Sequence, Archaea/enzymology/genetics, Bacteria/enzymology/genetics, Catalytic Domain, Chlorobi/enzymology/genetics, Crystallography; X-Ray, Dimerization, Electrostatics, Enzyme Stability, L-Lactate Dehydrogenase/chemistry/genetics, Malate Dehydrogenase/*chemistry, Models; Molecular, Molecular Sequence Data, Protein Conformation, Protein Structure; Quaternary, Protein Subunits, Recombinant Proteins/chemistry/genetics, Sequence Homology; Amino Acid, Temperature
Nationell ämneskategori
Strukturbiologi
Identifikatorer
URN: urn:nbn:se:umu:diva-17927PubMedID: 12054817OAI: oai:DiVA.org:umu-17927DiVA, id: diva2:157600
Tillgänglig från: 2007-11-23 Skapad: 2007-11-23 Senast uppdaterad: 2018-06-09Bibliografiskt granskad

Open Access i DiVA

Fulltext saknas i DiVA

Övriga länkar

PubMedhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Retrieve&list_uids=12054817&dopt=Citation

Person

Sauer, Uwe

Sök vidare i DiVA

Av författaren/redaktören
Sauer, Uwe
Av organisationen
Umeå centrum för molekylär patogenes (UCMP) (Teknisk-naturvetenskaplig fakultet)
Strukturbiologi

Sök vidare utanför DiVA

GoogleGoogle Scholar

pubmed
urn-nbn

Altmetricpoäng

pubmed
urn-nbn
Totalt: 724 träffar
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf