1zmo
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1zmt|1ZMT]], [[1zo8|1ZO8]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zmo OCA], [http://www.ebi.ac.uk/pdbsum/1zmo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zmo RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ZMO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arthrobacter_sp. | + | 1ZMO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arthrobacter_sp._ad2 Arthrobacter sp. ad2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZMO OCA]. |
==Reference== | ==Reference== | ||
The X-ray structure of the haloalcohol dehalogenase HheA from Arthrobacter sp. strain AD2: insight into enantioselectivity and halide binding in the haloalcohol dehalogenase family., de Jong RM, Kalk KH, Tang L, Janssen DB, Dijkstra BW, J Bacteriol. 2006 Jun;188(11):4051-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16707696 16707696] | The X-ray structure of the haloalcohol dehalogenase HheA from Arthrobacter sp. strain AD2: insight into enantioselectivity and halide binding in the haloalcohol dehalogenase family., de Jong RM, Kalk KH, Tang L, Janssen DB, Dijkstra BW, J Bacteriol. 2006 Jun;188(11):4051-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16707696 16707696] | ||
| - | [[Category: Arthrobacter sp. | + | [[Category: Arthrobacter sp. ad2]] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dijkstra, B W.]] | [[Category: Dijkstra, B W.]] | ||
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[[Category: short-chain dehydrogenase/reductase family]] | [[Category: short-chain dehydrogenase/reductase family]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:38:49 2008'' |
Revision as of 22:38, 30 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Related: | 1ZMT, 1ZO8
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Apo structure of haloalcohol dehalogenase HheA of Arthrobacter sp. AD2
Overview
Haloalcohol dehalogenases are bacterial enzymes that cleave the carbon-halogen bond in short aliphatic vicinal haloalcohols, like 1-chloro-2,3-propanediol, some of which are recalcitrant environmental pollutants. They use a conserved Ser-Tyr-Arg catalytic triad to deprotonate the haloalcohol oxygen, which attacks the halogen-bearing carbon atom, producing an epoxide and a halide ion. Here, we present the X-ray structure of the haloalcohol dehalogenase HheA(AD2) from Arthrobacter sp. strain AD2 at 2.0-A resolution. Comparison with the previously reported structure of the 34% identical enantioselective haloalcohol dehalogenase HheC from Agrobacterium radiobacter AD1 shows that HheA(AD2) has a similar quaternary and tertiary structure but a much more open substrate-binding pocket. Docking experiments reveal that HheA(AD2) can bind both enantiomers of the haloalcohol substrate 1-p-nitrophenyl-2-chloroethanol in a productive way, which explains the low enantiopreference of HheA(AD2). Other differences are found in the halide-binding site, where the side chain amino group of Asn182 is in a position to stabilize the halogen atom or halide ion in HheA(AD2), in contrast to HheC, where a water molecule has taken over this role. These results broaden the insight into the structural determinants that govern reactivity and selectivity in the haloalcohol dehalogenase family.
About this Structure
1ZMO is a Single protein structure of sequence from Arthrobacter sp. ad2. Full crystallographic information is available from OCA.
Reference
The X-ray structure of the haloalcohol dehalogenase HheA from Arthrobacter sp. strain AD2: insight into enantioselectivity and halide binding in the haloalcohol dehalogenase family., de Jong RM, Kalk KH, Tang L, Janssen DB, Dijkstra BW, J Bacteriol. 2006 Jun;188(11):4051-6. PMID:16707696
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