2j7q
From Proteopedia
(Difference between revisions)
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<StructureSection load='2j7q' size='340' side='right' caption='[[2j7q]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='2j7q' size='340' side='right' caption='[[2j7q]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | [[2j7q]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Murid_herpesvirus_1 Murid herpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J7Q OCA]. <br> | + | <table><tr><td colspan='2'>[[2j7q]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Murid_herpesvirus_1 Murid herpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J7Q OCA]. <br> |
| - | <b>[[Ligand|Ligands:]]</b> <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GVE:METHYL+4-AMINOBUTANOATE'>GVE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene><br> | + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GVE:METHYL+4-AMINOBUTANOATE'>GVE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene><br> |
| - | <b>[[Non-Standard_Residue|NonStd Res:]]</b> <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>< | + | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <b>[[Related_structure|Related:]]</b> [[1c3t|1c3t]], [[1d3z|1d3z]], [[1f9j|1f9j]], [[1fxt|1fxt]], [[1g6j|1g6j]], [[1gjz|1gjz]], [[1nbf|1nbf]], [[1ogw|1ogw]], [[1q5w|1q5w]], [[1s1q|1s1q]], [[1sif|1sif]], [[1tbe|1tbe]], [[1ubi|1ubi]], [[1ubq|1ubq]], [[1xd3|1xd3]], [[1xqq|1xqq]], [[1yx5|1yx5]], [[1yx6|1yx6]], [[1zgu|1zgu]], [[2ayo|2ayo]], [[2bgf|2bgf]], [[2fcm|2fcm]], [[2fcn|2fcn]], [[2fcq|2fcq]], [[2fcs|2fcs]], [[2fuh|2fuh]], [[2g45|2g45]], [[2gbk|2gbk]], [[2gbm|2gbm]], [[2gbn|2gbn]]< | + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1c3t|1c3t]], [[1d3z|1d3z]], [[1f9j|1f9j]], [[1fxt|1fxt]], [[1g6j|1g6j]], [[1gjz|1gjz]], [[1nbf|1nbf]], [[1ogw|1ogw]], [[1q5w|1q5w]], [[1s1q|1s1q]], [[1sif|1sif]], [[1tbe|1tbe]], [[1ubi|1ubi]], [[1ubq|1ubq]], [[1xd3|1xd3]], [[1xqq|1xqq]], [[1yx5|1yx5]], [[1yx6|1yx6]], [[1zgu|1zgu]], [[2ayo|2ayo]], [[2bgf|2bgf]], [[2fcm|2fcm]], [[2fcn|2fcn]], [[2fcq|2fcq]], [[2fcs|2fcs]], [[2fuh|2fuh]], [[2g45|2g45]], [[2gbk|2gbk]], [[2gbm|2gbm]], [[2gbn|2gbn]]</td></tr> |
| - | <b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span>< | + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> |
| - | <b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j7q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2j7q RCSB], [http://www.ebi.ac.uk/pdbsum/2j7q PDBsum]</span>< | + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j7q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2j7q RCSB], [http://www.ebi.ac.uk/pdbsum/2j7q PDBsum]</span></td></tr> |
| + | <table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| - | [[Image:Consurf_key_small.gif|right]] | + | [[Image:Consurf_key_small.gif|200px|right]] |
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
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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/chain_selection.php?pdb_ID=2ata 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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
All members of the herpesviridae contain within their large tegument protein a cysteine protease module that displays deubiquitinating activity. We report the crystal structure of the cysteine protease domain of murine cytomegalovirus M48 (M48(USP)) in a complex with a ubiquitin (Ub)-based suicide substrate. M48(USP) adopts a papain-like fold, with the active-site cysteine forming a thioether linkage to the suicide substrate. The Ub core participates in an extensive hydrophobic interaction with an exposed beta hairpin loop of M48(USP). This Ub binding mode contributes to Ub specificity and is distinct from that observed in other deubiquitinating enzymes. Both the arrangement of active-site residues and the architecture of the interface with Ub lead us to classify this domain as the founding member of a previously unknown class of deubiquitinating enzymes. | All members of the herpesviridae contain within their large tegument protein a cysteine protease module that displays deubiquitinating activity. We report the crystal structure of the cysteine protease domain of murine cytomegalovirus M48 (M48(USP)) in a complex with a ubiquitin (Ub)-based suicide substrate. M48(USP) adopts a papain-like fold, with the active-site cysteine forming a thioether linkage to the suicide substrate. The Ub core participates in an extensive hydrophobic interaction with an exposed beta hairpin loop of M48(USP). This Ub binding mode contributes to Ub specificity and is distinct from that observed in other deubiquitinating enzymes. Both the arrangement of active-site residues and the architecture of the interface with Ub lead us to classify this domain as the founding member of a previously unknown class of deubiquitinating enzymes. | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:58, 1 May 2014
CRYSTAL STRUCTURE OF THE UBIQUITIN-SPECIFIC PROTEASE ENCODED BY MURINE CYTOMEGALOVIRUS TEGUMENT PROTEIN M48 IN COMPLEX WITH A UBQUITIN-BASED SUICIDE SUBSTRATE
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