1yd6: Difference between revisions

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[[Image:1yd6.gif|left|200px]]


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==Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Bacillus caldotenax==
The line below this paragraph, containing "STRUCTURE_1yd6", creates the "Structure Box" on the page.
<StructureSection load='1yd6' size='340' side='right'caption='[[1yd6]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1yd6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_caldotenax Bacillus caldotenax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YD6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YD6 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_1yd6| PDB=1yd6 |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yd6 OCA], [https://pdbe.org/1yd6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yd6 RCSB], [https://www.ebi.ac.uk/pdbsum/1yd6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yd6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UVRC_GEOKA UVRC_GEOKA] The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.[HAMAP-Rule:MF_00203]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yd/1yd6_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1yd6 ConSurf].
<div style="clear:both"></div>


'''Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Bacillus caldotenax'''
==See Also==
 
*[[UvrABC|UvrABC]]
 
__TOC__
==Overview==
</StructureSection>
Nucleotide excision repair is a highly conserved DNA repair mechanism present in all kingdoms of life. The incision reaction is a critical step for damage removal and is accomplished by the UvrC protein in eubacteria. No structural information is so far available for the 3' incision reaction. Here we report the crystal structure of the N-terminal catalytic domain of UvrC at 1.5 A resolution, which catalyzes the 3' incision reaction and shares homology with the catalytic domain of the GIY-YIG family of intron-encoded homing endonucleases. The structure reveals a patch of highly conserved residues surrounding a catalytic magnesium-water cluster, suggesting that the metal binding site is an essential feature of UvrC and all GIY-YIG endonuclease domains. Structural and biochemical data strongly suggest that the N-terminal endonuclease domain of UvrC utilizes a novel one-metal mechanism to cleave the phosphodiester bond.
[[Category: Large Structures]]
 
[[Category: Croteau DL]]
==About this Structure==
[[Category: DellaVecchia MJ]]
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YD6 OCA].
[[Category: Karakas E]]
 
[[Category: Kisker C]]
==Reference==
[[Category: Rhau B]]
Structural insights into the first incision reaction during nucleotide excision repair., Truglio JJ, Rhau B, Croteau DL, Wang L, Skorvaga M, Karakas E, DellaVecchia MJ, Wang H, Van Houten B, Kisker C, EMBO J. 2005 Mar 9;24(5):885-94. Epub 2005 Feb 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15692561 15692561]
[[Category: Skorvaga M]]
[[Category: Croteau, D L.]]
[[Category: Truglio JJ]]
[[Category: DellaVecchia, M J.]]
[[Category: Van Houten B]]
[[Category: Houten, B Van.]]
[[Category: Wang H]]
[[Category: Karakas, E.]]
[[Category: Wang L]]
[[Category: Kisker, C.]]
[[Category: Rhau, B.]]
[[Category: Skorvaga, M.]]
[[Category: Truglio, J J.]]
[[Category: Wang, H.]]
[[Category: Wang, L.]]
[[Category: Dna binding protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:10:36 2008''

Latest revision as of 16:37, 13 March 2024

Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Bacillus caldotenaxCrystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Bacillus caldotenax

Structural highlights

1yd6 is a 4 chain structure with sequence from Bacillus caldotenax. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

UVRC_GEOKA The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.[HAMAP-Rule:MF_00203]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1yd6, resolution 2.00Å

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