|
|
| Line 1: |
Line 1: |
| | | | |
| | ==The X-ray structure of Hahella chejuensis family 48 glycosyl hydrolase== | | ==The X-ray structure of Hahella chejuensis family 48 glycosyl hydrolase== |
| - | <StructureSection load='4fus' size='340' side='right' caption='[[4fus]], [[Resolution|resolution]] 1.75Å' scene=''> | + | <StructureSection load='4fus' size='340' side='right'caption='[[4fus]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4fus]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hahch Hahch]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FUS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FUS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4fus]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hahella_chejuensis_KCTC_2396 Hahella chejuensis KCTC 2396]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FUS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CBI:CELLOBIOSE'>CBI</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OHI:3-(2-OXO-2H-IMIDAZOL-4-YL)-L-ALANINE'>OHI</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PRD_900005:beta-cellobiose'>PRD_900005</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OHI:3-(2-OXO-2H-IMIDAZOL-4-YL)-L-ALANINE'>OHI</scene></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=4fus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fus OCA], [https://pdbe.org/4fus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fus RCSB], [https://www.ebi.ac.uk/pdbsum/4fus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fus ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HCH_02465 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=349521 HAHCH])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></td></tr> | + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fus OCA], [http://pdbe.org/4fus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fus RCSB], [http://www.ebi.ac.uk/pdbsum/4fus PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fus ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q2SJA2_HAHCH Q2SJA2_HAHCH] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cellulase]] | + | [[Category: Hahella chejuensis KCTC 2396]] |
| - | [[Category: Hahch]] | + | [[Category: Large Structures]] |
| - | [[Category: Alahuhta, P M]] | + | [[Category: Alahuhta PM]] |
| - | [[Category: Lunin, V V]] | + | [[Category: Lunin VV]] |
| - | [[Category: Gh48]]
| + | |
| - | [[Category: Glycosyl hydrolase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
4fus is a 1 chain structure with sequence from Hahella chejuensis KCTC 2396. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q2SJA2_HAHCH
Publication Abstract from PubMed
Currently, the cost of cellulase enzymes remains a key economic impediment to commercialization of biofuels (1). Enzymes from glycoside hydrolase family 48 (GH48) are a critical component of numerous natural lignocellulose-degrading systems. Although computational mining of large genomic data sets is a promising new approach for identifying novel cellulolytic activities, current computational methods are unable to distinguish between cellulases and enzymes with different substrate specificities that belong to the same protein family. We show that by using a robust computational approach supported by experimental studies, cellulases and non-cellulases can be effectively identified within a given protein family. Phylogenetic analysis of GH48 showed non-monophyletic distribution, an indication of horizontal gene transfer. Enzymatic function of GH48 proteins coded by horizontally transferred genes was verified experimentally, which confirmed that these proteins are cellulases. Computational and structural studies of GH48 enzymes identified structural elements that define cellulases and can be used to computationally distinguish them from non-cellulases. We propose that the structural element that can be used for in silico discrimination between cellulases and non-cellulases belonging to GH48 is an omega-loop located on the surface of the molecule and characterized by highly conserved rare amino acids. These markers were used to screen metagenomics data for "true" cellulases.
Sequence, structure, and evolution of cellulases in glycoside hydrolase family 48.,Sukharnikov LO, Alahuhta M, Brunecky R, Upadhyay A, Himmel ME, Lunin VV, Zhulin IB J Biol Chem. 2012 Nov 30;287(49):41068-77. doi: 10.1074/jbc.M112.405720. Epub, 2012 Oct 10. PMID:23055526[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sukharnikov LO, Alahuhta M, Brunecky R, Upadhyay A, Himmel ME, Lunin VV, Zhulin IB. Sequence, structure, and evolution of cellulases in glycoside hydrolase family 48. J Biol Chem. 2012 Nov 30;287(49):41068-77. doi: 10.1074/jbc.M112.405720. Epub, 2012 Oct 10. PMID:23055526 doi:http://dx.doi.org/10.1074/jbc.M112.405720
|
