4tq1

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<StructureSection load='4tq1' size='340' side='right'caption='[[4tq1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='4tq1' size='340' side='right'caption='[[4tq1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4tq1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TQ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TQ1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4tq1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TQ1 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tq0|4tq0]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.802&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ATG5, APG5L, ASP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), TECPR1, KIAA1358 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4tq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tq1 OCA], [https://pdbe.org/4tq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tq1 RCSB], [https://www.ebi.ac.uk/pdbsum/4tq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tq1 ProSAT]</span></td></tr>
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<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=4tq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tq1 OCA], [http://pdbe.org/4tq1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tq1 RCSB], [http://www.ebi.ac.uk/pdbsum/4tq1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tq1 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ATG5_HUMAN ATG5_HUMAN]] Involved in autophagy vesicles formation. Conjugation with ATG12 through an ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. Involved in mitochondrial quality control after oxidative damage, and in subsequent cellular longevity. The ATG12-ATG5 conjugate also regulates negatively the innate antiviral immune response by blocking the type I IFN production pathway through direct association with RARRES3 and MAVS. Plays also a role in translation or delivery of incoming viral RNA to the translation apparatus. HCV utilizes ATG5 as a proviral factor during the onset of viral infection. Plays a critical role in multiple aspects of lymphocyte development and is essential for both B and T lymphocyte survival and proliferation. Required for optimal processing and presentation of antigens for MHC II. Involved in the maintenance of axon morphology and membrane structures; as well as in normal adipocyte differentiation.<ref>PMID:7796880</ref> <ref>PMID:12207896</ref> <ref>PMID:15778222</ref> <ref>PMID:17709747</ref> <ref>PMID:20580051</ref> <ref>PMID:22170153</ref> May play an important role in the apoptotic process, possibly within the modified cytoskeleton. Its expression is a relatively late event in the apoptotic process, occurring downstream of caspase activity. Plays a crucial role in IFN-gamma-induced autophagic cell death by interacting with FADD.<ref>PMID:7796880</ref> <ref>PMID:12207896</ref> <ref>PMID:15778222</ref> <ref>PMID:17709747</ref> <ref>PMID:20580051</ref> <ref>PMID:22170153</ref> [[http://www.uniprot.org/uniprot/TCPR1_HUMAN TCPR1_HUMAN]] Tethering factor involved in autophagy. Involved in autophagosome maturation by promoting the autophagosome fusion with lysosomes: acts by associating with both the ATG5-ATG12 conjugate and phosphatidylinositol-3-phosphate (PtdIns(3)P) present at the surface of autophagosomes. Also involved in selective autophagy against bacterial pathogens, by being required for phagophore/preautophagosomal structure biogenesis and maturation.<ref>PMID:21575909</ref> <ref>PMID:22342342</ref>
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[https://www.uniprot.org/uniprot/ATG5_HUMAN ATG5_HUMAN] Involved in autophagy vesicles formation. Conjugation with ATG12 through an ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. Involved in mitochondrial quality control after oxidative damage, and in subsequent cellular longevity. The ATG12-ATG5 conjugate also regulates negatively the innate antiviral immune response by blocking the type I IFN production pathway through direct association with RARRES3 and MAVS. Plays also a role in translation or delivery of incoming viral RNA to the translation apparatus. HCV utilizes ATG5 as a proviral factor during the onset of viral infection. Plays a critical role in multiple aspects of lymphocyte development and is essential for both B and T lymphocyte survival and proliferation. Required for optimal processing and presentation of antigens for MHC II. Involved in the maintenance of axon morphology and membrane structures; as well as in normal adipocyte differentiation.<ref>PMID:7796880</ref> <ref>PMID:12207896</ref> <ref>PMID:15778222</ref> <ref>PMID:17709747</ref> <ref>PMID:20580051</ref> <ref>PMID:22170153</ref> May play an important role in the apoptotic process, possibly within the modified cytoskeleton. Its expression is a relatively late event in the apoptotic process, occurring downstream of caspase activity. Plays a crucial role in IFN-gamma-induced autophagic cell death by interacting with FADD.<ref>PMID:7796880</ref> <ref>PMID:12207896</ref> <ref>PMID:15778222</ref> <ref>PMID:17709747</ref> <ref>PMID:20580051</ref> <ref>PMID:22170153</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Autophagy is a bulky catabolic process that responds to nutrient homeostasis and extracellular stress signals and is a conserved mechanism in all eukaryotes. When autophagy is induced, cellular components are sequestered within an autophagosome and finally degraded by subsequent fusion with a lysosome. During this process, the ATG12-ATG5 conjugate requires 2 different binding partners, ATG16L1 for autophagosome elongation and TECPR1 for lysosomal fusion. In our current study, we describe the crystal structures of human ATG5 in complex with an N-terminal domain of ATG16L1 as well as an internal AIR domain of TECPR1. Both binding partners exhibit a similar alpha-helical structure containing a conserved binding motif termed AFIM. Furthermore, we characterize the critical role of the C-terminal unstructured region of the AIR domain of TECPR1. These findings are further confirmed by biochemical and cell biological analyses. These results provide new insights into the molecular details of the autophagosome maturation process, from its elongation to its fusion with a lysosome.
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Insights into autophagosome maturation revealed by the structures of ATG5 with its interacting partners.,Kim JH, Hong SB, Lee JK, Han S, Roh KH, Lee KE, Kim YK, Choi EJ, Song HK Autophagy. 2015 Jan 2;11(1):75-87. doi: 10.4161/15548627.2014.984276. PMID:25484072<ref>PMID:25484072</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4tq1" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hong, S B]]
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[[Category: Hong SB]]
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[[Category: Kim, J H]]
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[[Category: Kim JH]]
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[[Category: Song, H K]]
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[[Category: Song HK]]
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[[Category: Autophagy protein complex]]
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[[Category: Protein binding]]
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Current revision

Crystal structure of human ATG5-TECAIR

PDB ID 4tq1

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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