5fgy: Difference between revisions

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<StructureSection load='5fgy' size='340' side='right'caption='[[5fgy]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='5fgy' size='340' side='right'caption='[[5fgy]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5fgy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ade02 Ade02]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FGY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FGY FirstGlance]. <br>
<table><tr><td colspan='2'>[[5fgy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_adenovirus_2 Human adenovirus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FGY FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1avp|1avp]]</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]] 2.1&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">L3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10515 ADE02])</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=5fgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fgy OCA], [https://pdbe.org/5fgy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fgy RCSB], [https://www.ebi.ac.uk/pdbsum/5fgy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fgy ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenain Adenain], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.39 3.4.22.39] </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=5fgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fgy OCA], [http://pdbe.org/5fgy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fgy RCSB], [http://www.ebi.ac.uk/pdbsum/5fgy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fgy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PRO_ADE02 PRO_ADE02]] Cleaves viral precursor proteins (pTP, pIIIa, pVI, pVII, pVIII, and pX) inside newly assembled particles giving rise to mature virions. Protease complexed to its cofactor slides along the viral DNA to specifically locate and cleave the viral precursors. Mature virions have a weakened organization compared to the unmature virions, thereby facilitating subsequent uncoating. Without maturation, the particle lacks infectivity and is unable to uncoat. Late in adenovirus infection, in the cytoplasm, may participate in the cytoskeleton destruction. Cleaves host cells cytoskeletal keratins K7 and K18.<ref>PMID:22791715</ref>
[https://www.uniprot.org/uniprot/PRO_ADE02 PRO_ADE02] Cleaves viral precursor proteins (pTP, pIIIa, pVI, pVII, pVIII, and pX) inside newly assembled particles giving rise to mature virions. Protease complexed to its cofactor slides along the viral DNA to specifically locate and cleave the viral precursors. Mature virions have a weakened organization compared to the unmature virions, thereby facilitating subsequent uncoating. Without maturation, the particle lacks infectivity and is unable to uncoat. Late in adenovirus infection, in the cytoplasm, may participate in the cytoskeleton destruction. Cleaves host cells cytoskeletal keratins K7 and K18.<ref>PMID:22791715</ref>  
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ade02]]
[[Category: Homo sapiens]]
[[Category: Adenain]]
[[Category: Human adenovirus 2]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Davis, R R]]
[[Category: Davis RR]]
[[Category: Hollis, T]]
[[Category: Hollis T]]
[[Category: Martinez, P]]
[[Category: Martinez P]]
[[Category: Cofactor]]
[[Category: Complex]]
[[Category: Hydrolase]]
[[Category: Protease]]

Latest revision as of 06:50, 19 July 2023

Structure of human adenovirus 2 protease with cofactor pVIC

5fgy, resolution 2.10Å

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