1h3g
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1h3g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Flavobacterium_sp._92 Flavobacterium sp. 92]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H3G FirstGlance]. <br> | <table><tr><td colspan='2'>[[1h3g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Flavobacterium_sp._92 Flavobacterium sp. 92]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H3G FirstGlance]. <br> | ||
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h3g OCA], [https://pdbe.org/1h3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h3g RCSB], [https://www.ebi.ac.uk/pdbsum/1h3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h3g ProSAT]</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=1h3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h3g OCA], [https://pdbe.org/1h3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h3g RCSB], [https://www.ebi.ac.uk/pdbsum/1h3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h3g ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q8KKG0_9FLAO Q8KKG0_9FLAO] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1h3g ConSurf]. | </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=1h3g ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Starting with oligopeptide sequences and using PCR, the gene of the cyclodextrinase from Flavobacterium sp. no. 92 was derived from the genomic DNA. The gene was sequenced and expressed in Escherichia coli; the gene product was purified and crystallized. An X-ray diffraction analysis using seleno-methionines with multiwavelength anomalous diffraction techniques yielded the refined 3D structure at 2.1 A resolution. The enzyme hydrolyzes alpha(1,4)-glycosidic bonds of cyclodextrins and linear malto-oligosaccharides. It belongs to the glycosylhydrolase family no. 13 and has a chain fold similar to that of alpha-amylases, cyclodextrin glycosyltransferases, and other cyclodextrinases. In contrast with most family members but in agreement with other cyclodextrinases, the enzyme contains an additional characteristic N-terminal domain of about 100 residues. This domain participates in the formation of a putative D2-symmetric tetramer but not in cyclodextrin binding at the active center as observed with the other cyclodextrinases. Moreover, the domain is located at a position quite different from that of the other cyclodextrinases. Whether oligomerization facilitates the cyclodextrin deformation required for hydrolysis is discussed. | ||
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| - | Covalent and three-dimensional structure of the cyclodextrinase from Flavobacterium sp. no. 92.,Fritzsche HB, Schwede T, Schulz GE Eur J Biochem. 2003 May;270(10):2332-41. PMID:12752453<ref>PMID:12752453</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1h3g" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Cyclomaltodextrinase]] | ||
[[Category: Flavobacterium sp. 92]] | [[Category: Flavobacterium sp. 92]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Fritzsche | + | [[Category: Fritzsche HB]] |
| - | [[Category: Jelakovic | + | [[Category: Jelakovic S]] |
| - | [[Category: Schulz | + | [[Category: Schulz GE]] |
| - | [[Category: Schwede | + | [[Category: Schwede T]] |
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Revision as of 11:27, 27 March 2024
Cyclomaltodextrinase from Flavobacterium sp. No. 92: from DNA sequence to protein structure
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