3aal: Difference between revisions
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[[ | ==Crystal Structure of endonuclease IV from Geobacillus kaustophilus== | ||
<StructureSection load='3aal' size='340' side='right' caption='[[3aal]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3aal]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Geobacillus_kaustophilus Geobacillus kaustophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AAL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AAL FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3aam|3aam]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GK2474 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1462 Geobacillus kaustophilus])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Deoxyribonuclease_IV_(phage-T(4)-induced) Deoxyribonuclease IV (phage-T(4)-induced)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.2 3.1.21.2] </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=3aal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aal OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aal RCSB], [http://www.ebi.ac.uk/pdbsum/3aal PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Endonuclease IV (EndoIV) is an endonuclease that acts at apurinic/apyrimidinic (AP) sites and is classified as either long-type or short-type. The crystal structures of representative types of EndoIV from Geobacillus kaustophilus and Thermus thermophilus HB8 were determined using X-ray crystallography. G. kaustophilus EndoIV (the long type) had a higher affinity for double-stranded DNA containing an AP-site analogue than T. thermophilus EndoIV (the short type). Structural analysis of the two different EndoIVs suggested that a C-terminal DNA-recognition loop that is only present in the long type contributes to its high affinity for AP sites. A mutation analysis showed that Lys267 in the C-terminal DNA-recognition loop plays an important role in DNA binding. | |||
An additional C-terminal loop in endonuclease IV, an apurinic/apyrimidinic endonuclease, controls binding affinity to DNA.,Asano R, Ishikawa H, Nakane S, Nakagawa N, Kuramitsu S, Masui R Acta Crystallogr D Biol Crystallogr. 2011 Mar;67(Pt 3):149-55. Epub 2011, Feb 15. PMID:21358045<ref>PMID:21358045</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Geobacillus kaustophilus]] | [[Category: Geobacillus kaustophilus]] | ||
[[Category: Asano, R.]] | [[Category: Asano, R.]] |
Revision as of 15:00, 29 October 2014
Crystal Structure of endonuclease IV from Geobacillus kaustophilusCrystal Structure of endonuclease IV from Geobacillus kaustophilus
Structural highlights
Publication Abstract from PubMedEndonuclease IV (EndoIV) is an endonuclease that acts at apurinic/apyrimidinic (AP) sites and is classified as either long-type or short-type. The crystal structures of representative types of EndoIV from Geobacillus kaustophilus and Thermus thermophilus HB8 were determined using X-ray crystallography. G. kaustophilus EndoIV (the long type) had a higher affinity for double-stranded DNA containing an AP-site analogue than T. thermophilus EndoIV (the short type). Structural analysis of the two different EndoIVs suggested that a C-terminal DNA-recognition loop that is only present in the long type contributes to its high affinity for AP sites. A mutation analysis showed that Lys267 in the C-terminal DNA-recognition loop plays an important role in DNA binding. An additional C-terminal loop in endonuclease IV, an apurinic/apyrimidinic endonuclease, controls binding affinity to DNA.,Asano R, Ishikawa H, Nakane S, Nakagawa N, Kuramitsu S, Masui R Acta Crystallogr D Biol Crystallogr. 2011 Mar;67(Pt 3):149-55. Epub 2011, Feb 15. PMID:21358045[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Geobacillus kaustophilus
- Asano, R.
- Ishikawa, H.
- Kuramitsu, S.
- Masui, R.
- Nakagawa, N.
- Nakane, S.
- RSGI, RIKEN Structural Genomics/Proteomics Initiative.
- Base excision repair
- Dna damage
- Dna repair
- Endoiv
- Endonuclease
- Hydrolase
- Metal-binding
- National project on protein structural and functional analyse
- Nppsfa
- Nuclease
- Riken structural genomics/proteomics initiative
- Rsgi
- Structural genomic
- Tim barrel