1jvb
From Proteopedia
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| - | [[Image:1jvb.gif|left|200px]]<br /> | + | [[Image:1jvb.gif|left|200px]]<br /><applet load="1jvb" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1jvb" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1jvb, resolution 1.85Å" /> | caption="1jvb, resolution 1.85Å" /> | ||
'''ALCOHOL DEHYDROGENASE FROM THE ARCHAEON SULFOLOBUS SOLFATARICUS'''<br /> | '''ALCOHOL DEHYDROGENASE FROM THE ARCHAEON SULFOLOBUS SOLFATARICUS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1JVB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. 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] | + | 1JVB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. 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 Sites: <scene name='pdbsite=ZNC:Residues That Bind A Structural Zn Ion (Zn A 400) In The ...'>ZNC</scene> and <scene name='pdbsite=ZNS:Residues That Bind The Catalytic Zn Ion (Zn A 500)'>ZNS</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JVB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 16:39:26 2007'' |
Revision as of 14:29, 18 December 2007
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ALCOHOL DEHYDROGENASE FROM THE ARCHAEON SULFOLOBUS SOLFATARICUS
Overview
The crystal structure of a medium-chain NAD(H)-dependent alcohol, dehydrogenase (ADH) from an archaeon has been solved by multiwavelength, anomalous diffraction, using a selenomethionine-substituted enzyme. The, protein (SsADH), extracted from the hyperthermophilic organism Sulfolobus, solfataricus, is a homo-tetramer with a crystallographic 222 symmetry., Despite the low level of sequence identity, the overall fold of the, monomer is similar to that of the other homologous ADHs of known, structure. However, a significant difference is the orientation of the, catalytic domain relative to the coenzyme-binding domain that results in a, larger interdomain cleft. At the bottom of this cleft, the catalytic zinc, ion is coordinated tetrahedrally and lacks the zinc-bound water molecule, that is usually found in ADH apoform structures. The fourth coordination, position is indeed occupied by a Glu residue, as found in bacterial, tetrameric ADHs. Other differences are found in the architecture of the, substrate pocket whose entrance is more restricted than in other ADHs., SsADH is the first tetrameric ADH X-ray structure containing a second zinc, ion playing a structural role. This latter metal ion shows a peculiar, coordination, with a glutamic acid residue replacing one of the four, cysteine ligands that are highly conserved throughout the structural, zinc-containing dimeric ADHs.
About this Structure
1JVB is a Single protein structure of sequence from Sulfolobus solfataricus with ZN as ligand. Active as Alcohol dehydrogenase, with EC number 1.1.1.1 Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
Crystal structure of the alcohol dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus at 1.85 A resolution., Esposito L, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A, J Mol Biol. 2002 Apr 26;318(2):463-77. PMID:12051852
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