1bix
From Proteopedia
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|PDB= 1bix |SIZE=350|CAPTION= <scene name='initialview01'>1bix</scene>, resolution 2.2Å | |PDB= 1bix |SIZE=350|CAPTION= <scene name='initialview01'>1bix</scene>, resolution 2.2Å | ||
|SITE= <scene name='pdbsite=ROX:CYS+65+Has+Been+Proposed+To+Be+Involved+In+The+Reductive+...'>ROX</scene> | |SITE= <scene name='pdbsite=ROX:CYS+65+Has+Been+Proposed+To+Be+Involved+In+The+Reductive+...'>ROX</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene>, <scene name='pdbligand=SM:SAMARIUM+(III)+ION'>SM</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/DNA-(apurinic_or_apyrimidinic_site)_lyase DNA-(apurinic or apyrimidinic site) lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.99.18 4.2.99.18] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-(apurinic_or_apyrimidinic_site)_lyase DNA-(apurinic or apyrimidinic site) lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.99.18 4.2.99.18] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bix OCA], [http://www.ebi.ac.uk/pdbsum/1bix PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bix RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
The structure of the major human apurinic/ apyrimidinic endonuclease (HAP1) has been solved at 2.2 A resolution. The enzyme consists of two symmetrically related domains of similar topology and has significant structural similarity to both bovine DNase I and its Escherichia coli homologue exonuclease III (EXOIII). A structural comparison of these enzymes reveals three loop regions specific to HAP1 and EXOIII. These loop regions apparently act in DNA abasic site (AP) recognition and cleavage since DNase I, which lacks these loops, correspondingly lacks AP site specificity. The HAP1 structure furthermore suggests a mechanism for AP site binding which involves the recognition of the deoxyribose moiety in an extrahelical conformation, rather than a 'flipped-out' base opposite the AP site. | The structure of the major human apurinic/ apyrimidinic endonuclease (HAP1) has been solved at 2.2 A resolution. The enzyme consists of two symmetrically related domains of similar topology and has significant structural similarity to both bovine DNase I and its Escherichia coli homologue exonuclease III (EXOIII). A structural comparison of these enzymes reveals three loop regions specific to HAP1 and EXOIII. These loop regions apparently act in DNA abasic site (AP) recognition and cleavage since DNase I, which lacks these loops, correspondingly lacks AP site specificity. The HAP1 structure furthermore suggests a mechanism for AP site binding which involves the recognition of the deoxyribose moiety in an extrahelical conformation, rather than a 'flipped-out' base opposite the AP site. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Autoimmune polyglandular disease, type I OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607358 607358]], Sveinsson choreoretinal atrophy OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=189967 189967]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Rothwell, D G.]] | [[Category: Rothwell, D G.]] | ||
[[Category: Tainer, J A.]] | [[Category: Tainer, J A.]] | ||
| - | [[Category: PT]] | ||
| - | [[Category: SM]] | ||
[[Category: abasic site recognition]] | [[Category: abasic site recognition]] | ||
[[Category: dna repair]] | [[Category: dna repair]] | ||
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[[Category: ref-1]] | [[Category: ref-1]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:01:55 2008'' |
Revision as of 16:02, 30 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | DNA-(apurinic or apyrimidinic site) lyase, with EC number 4.2.99.18 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTAL STRUCTURE OF THE HUMAN DNA REPAIR ENDONUCLEASE HAP1 SUGGESTS THE RECOGNITION OF EXTRA-HELICAL DEOXYRIBOSE AT DNA ABASIC SITES
Overview
The structure of the major human apurinic/ apyrimidinic endonuclease (HAP1) has been solved at 2.2 A resolution. The enzyme consists of two symmetrically related domains of similar topology and has significant structural similarity to both bovine DNase I and its Escherichia coli homologue exonuclease III (EXOIII). A structural comparison of these enzymes reveals three loop regions specific to HAP1 and EXOIII. These loop regions apparently act in DNA abasic site (AP) recognition and cleavage since DNase I, which lacks these loops, correspondingly lacks AP site specificity. The HAP1 structure furthermore suggests a mechanism for AP site binding which involves the recognition of the deoxyribose moiety in an extrahelical conformation, rather than a 'flipped-out' base opposite the AP site.
About this Structure
1BIX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites., Gorman MA, Morera S, Rothwell DG, de La Fortelle E, Mol CD, Tainer JA, Hickson ID, Freemont PS, EMBO J. 1997 Nov 3;16(21):6548-58. PMID:9351835
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