Haloalkane dehalogenase LinB from Sphingomonas paucimobilis
UT26: X-ray crystallographic studies of dehalogenation of
brominated substrates

J 2003

Haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26: X-ray crystallographic studies of dehalogenation of brominated substrates

STRELTSOV, Victor, Zbyněk PROKOP, Jiří DAMBORSKÝ, Yuji NAGATA, Aaron OAKLEY et. al.

Základní údaje

Originální název

Haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26: X-ray crystallographic studies of dehalogenation of brominated substrates

Autoři

STRELTSOV, Victor (36 Austrálie), Zbyněk PROKOP (203 Česká republika), Jiří DAMBORSKÝ (203 Česká republika, garant), Yuji NAGATA (392 Japonsko), Aaron OAKLEY (36 Austrálie) a Matthew C.J. WILCE (36 Austrálie)

Vydání

Biochemistry, 2003, 0006-2960

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 3.922

Kód RIV

RIV/00216224:14310/03:00008998

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000186531100033

Klíčová slova anglicky

DEHALOGENASE X-RAY GC-MS

Štítky

DEHALOGENASE X-RAY GC-MS

Změněno: 19. 3. 2010 11:05, prof. Mgr. Jiří Damborský, Dr.

Anotace

V originále

The haloalkane dehalogenases are detoxifying enzymes that convert a broad range of halogenated substrates to the corresponding alcohols. Complete crystal structures of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 (LinB), and complexes of LinB with 1,2-propanediol/1-bromopropane-2-ol and 2-bromo-2-propene-1-ol, products of debromination of 1,2-dibromopropane and 2,3-dibromopropene, respectively, were determined from 1.8 A resolution X-ray diffraction data. Published structures of native LinB and its complex with 1,3-propanediol [Marek et al. (2000) Biochemistry 39, 14082-14086] were re-examined. The full and partial debromination of 1,2-dibromopropane and 2,3-dibromopropene, respectively, conformed to the observed general trend that the sp3-hybridized carbon is the predominant electrophilic site for the SN2 bimolecular nucleophilic substitution in dehalogenation reaction. The 2-bromo-2-propene-1-ol product of 2,3-dibromopropene dehalogenation in crystal was positively identified by the gas chromatography-mass spectroscopy (GC-MS) technique. The 1,2-propanediol and 1-bromopropane-2-ol products of 1,2-dibromopropane dehalogenation in crystal were also supported by the GC-MS identification. Comparison of native LinB with its complexes showed high flexibility of residues 136-157, in particular Asp146 and Glu147 from the cap domain helices a4 and a5'. Those residues were shifted mainly in direction towards the ligand molecules in the complex structures. It seems the cap domain moves nearer to the core squeezing substrate into the active center closer to the catalytic triad. This also leads to slight contraction of the whole complex structures. The flexibility detected by crystallographic analysis is in remarkable agreement with flexibility observed by molecular dynamic simulations.

Návaznosti

LN00A016, projekt VaV

Název: BIOMOLEKULÁRNÍ CENTRUM

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Biomolekulární centrum

Citovat

STRELTSOV, Victor, Zbyněk PROKOP, Jiří DAMBORSKÝ, Yuji NAGATA, Aaron OAKLEY a Matthew C.J. WILCE. Haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26: X-ray crystallographic studies of dehalogenation of brominated substrates. Biochemistry. 2003, roč. 42, č. 34, s. 10104-10112. ISSN 0006-2960.

@article{489638,
   author = {Streltsov, Victor and Prokop, Zbyněk and Damborský, Jiří and Nagata, Yuji and Oakley, Aaron and Wilce, Matthew C.J.},
   article_number = {34},
   keywords = {DEHALOGENASE X-RAY GC-MS},
   language = {eng},
   issn = {0006-2960},
   journal = {Biochemistry},
   title = {Haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26: X-ray crystallographic studies of dehalogenation of brominated substrates},
   url = {http://ncbr.chemi.muni.cz/~jiri/abstracts/biochem03a.html},
   volume = {42},
   year = {2003}
}

TY  - JOUR
ID  - 489638
AU  - Streltsov, Victor - Prokop, Zbyněk - Damborský, Jiří - Nagata, Yuji - Oakley, Aaron - Wilce, Matthew C.J.
PY  - 2003
TI  - Haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26: X-ray crystallographic studies of dehalogenation of brominated substrates
JF  - Biochemistry
VL  - 42
IS  - 34
SP  - 10104-10112
EP  - 10104-10112
SN  - 00062960
KW  - DEHALOGENASE X-RAY GC-MS
UR  - http://ncbr.chemi.muni.cz/~jiri/abstracts/biochem03a.html
N2  - The haloalkane dehalogenases are detoxifying enzymes that convert a broad range of halogenated substrates to the corresponding alcohols. Complete crystal structures of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 (LinB), and complexes of LinB with 1,2-propanediol/1-bromopropane-2-ol and 2-bromo-2-propene-1-ol, products of debromination of 1,2-dibromopropane and 2,3-dibromopropene, respectively, were determined from 1.8 A resolution X-ray diffraction data. Published structures of native LinB and its complex with 1,3-propanediol [Marek et al. (2000) Biochemistry 39, 14082-14086] were re-examined. The full and partial debromination of 1,2-dibromopropane and 2,3-dibromopropene, respectively, conformed to the observed general trend that the sp3-hybridized carbon is the predominant electrophilic site for the SN2 bimolecular nucleophilic substitution in dehalogenation reaction. The 2-bromo-2-propene-1-ol product of 2,3-dibromopropene dehalogenation in crystal was positively identified by the gas chromatography-mass spectroscopy (GC-MS) technique. The 1,2-propanediol and 1-bromopropane-2-ol products of 1,2-dibromopropane dehalogenation in crystal were also supported by the GC-MS identification. Comparison of native LinB with its complexes showed high flexibility of residues 136-157, in particular Asp146 and Glu147 from the cap domain helices a4 and a5'. Those residues were shifted mainly in direction towards the ligand molecules in the complex structures. It seems the cap domain moves nearer to the core squeezing substrate into the active center closer to the catalytic triad. This also leads to slight contraction of the whole complex structures. The flexibility detected by crystallographic analysis is in remarkable agreement with flexibility observed by molecular dynamic simulations.
ER  -

STRELTSOV, Victor, Zbyněk PROKOP, Jiří DAMBORSKÝ, Yuji NAGATA, Aaron OAKLEY a Matthew C.J. WILCE. Haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26: X-ray crystallographic studies of dehalogenation of brominated substrates. \textit{Biochemistry}. 2003, roč.~42, č.~34, s.~10104-10112. ISSN~0006-2960.

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