1h2b

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[[Image:1h2b.jpg|left|200px]]<br /><applet load="1h2b" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1h2b.jpg|left|200px]]
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caption="1h2b, resolution 1.62&Aring;" />
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'''CRYSTAL STRUCTURE OF THE ALCOHOL DEHYDROGENASE FROM THE HYPERTHERMOPHILIC ARCHAEON AEROPYRUM PERNIX AT 1.65A RESOLUTION'''<br />
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{{Structure
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|PDB= 1h2b |SIZE=350|CAPTION= <scene name='initialview01'>1h2b</scene>, resolution 1.62&Aring;
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|SITE= <scene name='pdbsite=OC1:Zn+Binding+Site+For+Chain+B,+Structural+Site'>OC1</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=OCA:OCTANOIC+ACID+(CAPRYLIC+ACID)'>OCA</scene> and <scene name='pdbligand=NAJ:NICOTINAMIDE-ADENINE-DINUCLEOTIDE (ACIDIC FORM)'>NAJ</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF THE ALCOHOL DEHYDROGENASE FROM THE HYPERTHERMOPHILIC ARCHAEON AEROPYRUM PERNIX AT 1.65A RESOLUTION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1H2B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=OCA:'>OCA</scene> and <scene name='pdbligand=NAJ:'>NAJ</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1] Known structural/functional Site: <scene name='pdbsite=OC1:Zn+Binding+Site+For+Chain+B,+Structural+Site'>OC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H2B OCA].
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1H2B is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H2B OCA].
==Reference==
==Reference==
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The structure of an alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix., Guy JE, Isupov MN, Littlechild JA, J Mol Biol. 2003 Aug 29;331(5):1041-51. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12927540 12927540]
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The structure of an alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix., Guy JE, Isupov MN, Littlechild JA, J Mol Biol. 2003 Aug 29;331(5):1041-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12927540 12927540]
[[Category: Aeropyrum pernix]]
[[Category: Aeropyrum pernix]]
[[Category: Alcohol dehydrogenase]]
[[Category: Alcohol dehydrogenase]]
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[[Category: zinc]]
[[Category: zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:56:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:31:11 2008''

Revision as of 09:31, 20 March 2008


PDB ID 1h2b

Drag the structure with the mouse to rotate
, resolution 1.62Å
Sites:
Ligands: , and
Activity: Alcohol dehydrogenase, with EC number 1.1.1.1
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE ALCOHOL DEHYDROGENASE FROM THE HYPERTHERMOPHILIC ARCHAEON AEROPYRUM PERNIX AT 1.65A RESOLUTION


Overview

The structure of the recombinant medium chain alcohol dehydrogenase (ADH) from the hyperthermophilic archaeon Aeropyrum pernix has been solved by the multiple anomalous dispersion technique using the signal from the naturally occurring zinc ions. The enzyme is a tetramer with 222 point group symmetry. The ADH monomer is formed from a catalytic and a cofactor-binding domain, with the overall fold similar to previously solved ADH structures. The 1.62 A resolution A.pernix ADH structure is that of the holo form, with the cofactor NADH bound into the cleft between the two domains. The electron density found in the active site has been interpreted to be octanoic acid, which has been shown to be an inhibitor of the enzyme. This inhibitor is positioned with its carbonyl oxygen atom forming the fourth ligand of the catalytic zinc ion. The structural zinc ion of each monomer is present at only partial occupancy and in its absence a disulfide bond is formed. The enhanced thermal stability of the A.pernix ADH is thought to arise primarily from increased ionic and hydrophobic interactions on the subunit interfaces.

About this Structure

1H2B is a Single protein structure of sequence from Aeropyrum pernix. Full crystallographic information is available from OCA.

Reference

The structure of an alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix., Guy JE, Isupov MN, Littlechild JA, J Mol Biol. 2003 Aug 29;331(5):1041-51. PMID:12927540

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