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| | <StructureSection load='1yq2' size='340' side='right'caption='[[1yq2]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='1yq2' size='340' side='right'caption='[[1yq2]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1yq2]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Arthrobacter_sp._c2-2 Arthrobacter sp. c2-2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQ2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1YQ2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1yq2]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Arthrobacter_sp._C2-2 Arthrobacter sp. C2-2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YQ2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LacZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=192168 Arthrobacter sp. C2-2])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </span></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=1yq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yq2 OCA], [https://pdbe.org/1yq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yq2 RCSB], [https://www.ebi.ac.uk/pdbsum/1yq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yq2 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1yq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yq2 OCA], [http://pdbe.org/1yq2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yq2 RCSB], [http://www.ebi.ac.uk/pdbsum/1yq2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yq2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8KRF6_9MICC Q8KRF6_9MICC] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arthrobacter sp. c2-2]] | + | [[Category: Arthrobacter sp. C2-2]] |
| - | [[Category: Beta-galactosidase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dohnalek, J]] | + | [[Category: Dohnalek J]] |
| - | [[Category: Hasek, J]] | + | [[Category: Hasek J]] |
| - | [[Category: Kralova, B]] | + | [[Category: Kralova B]] |
| - | [[Category: Lipovova, P]] | + | [[Category: Lipovova P]] |
| - | [[Category: Petrokova, H]] | + | [[Category: Petrokova H]] |
| - | [[Category: Skalova, T]] | + | [[Category: Skalova T]] |
| - | [[Category: Spiwok, V]] | + | [[Category: Spiwok V]] |
| - | [[Category: Strnad, H]] | + | [[Category: Strnad H]] |
| - | [[Category: Vondrackova, E]] | + | [[Category: Vondrackova E]] |
| - | [[Category: Glycosyl hydrolase family 2]]
| + | |
| - | [[Category: Hexamer]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Tim barrel]]
| + | |
| Structural highlights
1yq2 is a 6 chain structure with sequence from Arthrobacter sp. C2-2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.9Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q8KRF6_9MICC
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The X-ray structure of cold-active beta-galactosidase (isoenzyme C-2-2-1) from an Antarctic bacterium Arthrobacter sp. C2-2 was solved at 1.9A resolution. The enzyme forms 660 kDa hexamers with active sites opened to the central cavity of the hexamer and connected by eight channels with exterior solvent. To our best knowledge, this is the first cold-active beta-galactosidase with known structure and also the first known beta-galactosidase structure in the form of compact hexamers. The hexamer organization regulates access of substrates and ligands to six active sites and this unique packing, present also in solution, raises questions about its purpose and function. This enzyme belongs to glycosyl hydrolase family 2, similarly to Escherichia coli beta-galactosidase, forming tetramers necessary for its enzymatic function. However, we discovered significant differences between these two enzymes affecting the ability of tetramer/hexamer formation and complementation of the active site. This structure reveals new insights into the cold-adaptation mechanisms of enzymatic pathways of extremophiles.
Cold-active beta-galactosidase from Arthrobacter sp. C2-2 forms compact 660 kDa hexamers: crystal structure at 1.9A resolution.,Skalova T, Dohnalek J, Spiwok V, Lipovova P, Vondrackova E, Petrokova H, Duskova J, Strnad H, Kralova B, Hasek J J Mol Biol. 2005 Oct 21;353(2):282-94. PMID:16171818[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Skalova T, Dohnalek J, Spiwok V, Lipovova P, Vondrackova E, Petrokova H, Duskova J, Strnad H, Kralova B, Hasek J. Cold-active beta-galactosidase from Arthrobacter sp. C2-2 forms compact 660 kDa hexamers: crystal structure at 1.9A resolution. J Mol Biol. 2005 Oct 21;353(2):282-94. PMID:16171818 doi:10.1016/j.jmb.2005.08.028
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