Structural role of conserved Asn179 in the short-chain dehydrogenase/reductase scaffold

↓ Direkt till sidans innehåll
↓ Direkt till sidans sekundära innehåll (sidomenyn)

Sökning: WFRF:(Nordling C) > Structural role of ...

LIBRIS Formathandbok (Information om MARC21)

Fältnamn	Indikatorer	Metadata
000		03152naa a2200409 4500
001		oai:DiVA.org:sh-15836
003		SwePub
008		120309s2001 \| \|\|\|\|\|\|\|\|\|\|\|000 \|\|eng\|
009		oai:prod.swepub.kib.ki.se:1955179
024	7	a https://urn.kb.se/resolve?urn=urn:nbn:se:sh:diva-158362 URI
024	7	a https://doi.org/10.1006/bbrc.2001.60322 DOI
024	7	a http://kipublications.ki.se/Default.aspx?queryparsed=id:19551792 URI
040		a (SwePub)shd (SwePub)ki
041		a engb eng
042		9 SwePub
072	7	a ref2 swepub-contenttype
072	7	a art2 swepub-publicationtype
100	1	a Filling, C4 aut
245	1 0	a Structural role of conserved Asn179 in the short-chain dehydrogenase/reductase scaffold
264	1	b Elsevier BV,c 2001
338		a print2 rdacarrier
520		a Short-chain dehydrogenases/reductases (SDR) constitute a large family of enzymes found in all forms of life. Despite a low level of sequence identity, the three-dimensional structures determined display a nearly superimposable alpha/beta folding pattern. We identified a conserved asparagine residue located within strand betaF and analyzed its role in the short-chain dehydrogenase/reductase architecture. Mutagenetic replacement of Asn179 by Ala in bacterial 3 beta /17 beta -hydroxysteroid dehydrogenase yields a folded, but enzymatically inactive enzyme, which is significantly more resistant to denaturation by guanidinium hydrochloride. Crystallographic analysis of the wild-type enzyme at 1.2-Angstrom resolution reveals a hydrogen bonding network, including a buried and well-ordered water molecule connecting strands betaE to betaF, a common feature found in 16 of 21 known three-dimensional structures of the family. Based on these results, we hypothesize that in mammalian 11 beta -hydroxysteroid dehydrogenase the essential Asn-linked glycosylation site, which corresponds to the conserved segment, displays similar structural features and has a central role to maintain the SDR scaffold.
650	7	a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650	7	a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
650	7	a NATURVETENSKAPx Biologix Biofysik0 (SwePub)106032 hsv//swe
650	7	a NATURAL SCIENCESx Biological Sciencesx Biophysics0 (SwePub)106032 hsv//eng
700	1	a Nordling, E4 aut
700	1	a Benach, J4 aut
700	1	a Berndt, Kurt Du Karolinska Institutet,Södertörns högskola,Avdelning Naturvetenskap,Karolinska Institute4 aut0 (Swepub:sh)SHKTBT
700	1	a Ladenstein, Ru Karolinska Institutet4 aut
700	1	a Jörnvall, Hu Karolinska Institutet4 aut
700	1	a Oppermann, U4 aut
710	2	a Södertörns högskolab Avdelning Naturvetenskap4 org
773	0	t Biochemical and Biophysical Research Communications - BBRCd : Elsevier BVg 289:3, s. 712-717q 289:3<712-717x 0006-291Xx 1090-2104
856	4 8	u https://urn.kb.se/resolve?urn=urn:nbn:se:sh:diva-15836
856	4 8	u https://doi.org/10.1006/bbrc.2001.6032
856	4 8	u http://kipublications.ki.se/Default.aspx?queryparsed=id:1955179

Hitta via bibliotek

Biochemical and Biophysical Research Communications - BBRC (Sök värdpublikationen i LIBRIS)

Till lärosätets databas

Hitta mer i SwePub

Av författaren/redakt...: Filling, C; Nordling, E; Benach, J; Berndt, Kurt D; Ladenstein, R; Jörnvall, H; visa fler...; Oppermann, U; visa färre...

Om ämnet

NATURVETENSKAP: NATURVETENSKAP; och Biologi; och Biokemi och mole ...

NATURVETENSKAP: NATURVETENSKAP; och Biologi; och Biofysik

Artiklar i publikationen: Biochemical and ...

Av lärosätet: Södertörns högskola; Karolinska Institutet

Sök utanför SwePub

Sök vidare i:: Google; Google Book Search; Google Scholar

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

LIBRIS.kb.se