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| | <StructureSection load='1z0v' size='340' side='right'caption='[[1z0v]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='1z0v' size='340' side='right'caption='[[1z0v]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1z0v]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z0V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1z0v]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z0V FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1z0t|1z0t]], [[1z0g|1z0g]], [[1z0e|1z0e]], [[1z0b|1z0b]], [[1z0c|1z0c]], [[1z0w|1z0w]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1z0t|1z0t]], [[1z0g|1z0g]], [[1z0e|1z0e]], [[1z0b|1z0b]], [[1z0c|1z0c]], [[1z0w|1z0w]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] </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=1z0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z0v OCA], [http://pdbe.org/1z0v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z0v RCSB], [http://www.ebi.ac.uk/pdbsum/1z0v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z0v 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=1z0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z0v OCA], [https://pdbe.org/1z0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z0v RCSB], [https://www.ebi.ac.uk/pdbsum/1z0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z0v ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LONB_ARCFU LONB_ARCFU]] ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity). | + | [[https://www.uniprot.org/uniprot/LONB_ARCFU LONB_ARCFU]] ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Structural highlights
Function
[LONB_ARCFU] ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity).
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
Although macromolecular crystallography is rapidly becoming largely routine owing to advances in methods of data collection, structure solution and refinement, difficult cases are still common. To remind structural biologists about the kinds of crystallographic difficulties that might be encountered, case studies of several successfully completed structure determinations that utilized less than perfect crystals are discussed here. The structure of the proteolytic domain of Archaeoglobus fulgidus Lon was solved with crystals that contained superimposed orthorhombic and monoclinic lattices, a case not previously described for proteins. Another hexagonal crystal form of this protein exhibited an unusually high degree of non-isomorphism. Crystals of A. fulgidus Rio1 kinase exhibited both pseudosymmetry and twinning. Ways of identifying the observed phenomena and approaches to solving and refining macromolecular structures when only less than perfect crystals are available are discussed here.
Pathological crystallography: case studies of several unusual macromolecular crystals.,Dauter Z, Botos I, LaRonde-LeBlanc N, Wlodawer A Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):967-75. Epub 2005, Jun 24. PMID:15983420[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dauter Z, Botos I, LaRonde-LeBlanc N, Wlodawer A. Pathological crystallography: case studies of several unusual macromolecular crystals. Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):967-75. Epub 2005, Jun 24. PMID:15983420 doi:10.1107/S0907444905011285
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