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[[Image:1zmo.gif|left|200px]]
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{{STRUCTURE_1zmo|  PDB=1zmo  |  SCENE=  }}
'''Apo structure of haloalcohol dehalogenase HheA of Arthrobacter sp. AD2'''


==Apo structure of haloalcohol dehalogenase HheA of Arthrobacter sp. AD2==
<StructureSection load='1zmo' size='340' side='right'caption='[[1zmo]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1zmo]] is a 8 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZMO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zmo OCA], [https://pdbe.org/1zmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zmo RCSB], [https://www.ebi.ac.uk/pdbsum/1zmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zmo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q93MS3_9MICC Q93MS3_9MICC]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zm/1zmo_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zmo ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:16707696</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 1zmo" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Dehalogenase 3D structures|Dehalogenase 3D structures]]
[[Category: Arthrobacter sp. ad2]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Dijkstra, B W.]]
__TOC__
[[Category: Janssen, D B.]]
</StructureSection>
[[Category: Jong, R M.de.]]
[[Category: Arthrobacter sp. AD2]]
[[Category: Kalk, K H.]]
[[Category: Large Structures]]
[[Category: Tang, L.]]
[[Category: Dijkstra BW]]
[[Category: Haloalcohol dehalogenase]]
[[Category: Janssen DB]]
[[Category: Halohydrin dehalogenase]]
[[Category: Kalk KH]]
[[Category: Short-chain dehydrogenase/reductase family]]
[[Category: Tang L]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:48:57 2008''
[[Category: De Jong RM]]

Latest revision as of 07:11, 23 August 2023

Apo structure of haloalcohol dehalogenase HheA of Arthrobacter sp. AD2

1zmo, resolution 2.00Å

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