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[[Image:1ds0.jpg|left|200px]]


{{Structure
==CRYSTAL STRUCTURE OF CLAVAMINATE SYNTHASE==
|PDB= 1ds0 |SIZE=350|CAPTION= <scene name='initialview01'>1ds0</scene>, resolution 1.63&Aring;
<StructureSection load='1ds0' size='340' side='right'caption='[[1ds0]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
<table><tr><td colspan='2'>[[1ds0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DS0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DS0 FirstGlance]. <br>
|ACTIVITY=
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.63&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1ds0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ds0 OCA], [https://pdbe.org/1ds0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ds0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ds0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ds0 ProSAT]</span></td></tr>
 
</table>
'''CRYSTAL STRUCTURE OF CLAVAMINATE SYNTHASE'''
== Function ==
 
[https://www.uniprot.org/uniprot/CAS1_STRCL CAS1_STRCL]
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
Clavaminate synthase (CAS), a remarkable Fe(II)/2-oxoglutarate oxygenase, catalyzes three separate oxidative reactions in the biosynthesis of clavulanic acid, a clinically used inhibitor of serine beta-lactamases. The first CAS-catalyzed step (hydroxylation) is separated from the latter two (oxidative cyclization/desaturation) by the action of an amidinohydrolase. Here, we describe crystal structures of CAS in complex with Fe(II), 2-oxoglutarate (2OG) and substrates (N-alpha-acetyl-L-arginine and proclavaminic acid). They reveal how CAS catalyzes formation of the clavam nucleus, via a process unprecedented in synthetic organic chemistry, and suggest how it discriminates between substrates and controls reaction of its highly reactive ferryl intermediate. The presence of an unpredicted jelly roll beta-barrel core in CAS implies divergent evolution within the family of 2OG and related oxygenases. Comparison with other non-heme oxidases/oxygenases reveals flexibility in the position which dioxygen ligates to the iron, in contrast to the analogous heme-using enzymes.
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ds/1ds0_consurf.spt"</scriptWhenChecked>
1DS0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DS0 OCA].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==Reference==
  </jmolCheckbox>
Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase., Zhang Z, Ren J, Stammers DK, Baldwin JE, Harlos K, Schofield CJ, Nat Struct Biol. 2000 Feb;7(2):127-33. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10655615 10655615]
</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=1ds0 ConSurf].
[[Category: Single protein]]
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces clavuligerus]]
[[Category: Streptomyces clavuligerus]]
[[Category: Baldwin, J E.]]
[[Category: Baldwin JE]]
[[Category: Harlos, K.]]
[[Category: Harlos K]]
[[Category: Ren, J.]]
[[Category: Ren J]]
[[Category: Schofield, C J.]]
[[Category: Schofield CJ]]
[[Category: Stammers, D K.]]
[[Category: Stammers DK]]
[[Category: Zhang, Z H.]]
[[Category: Zhang ZH]]
[[Category: ACT]]
[[Category: SO4]]
[[Category: clavaminate synthase 1]]
[[Category: jelly roll]]
[[Category: oxygenase]]
[[Category: trifunctional enzyme]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:43:20 2008''

Latest revision as of 06:58, 7 February 2024

CRYSTAL STRUCTURE OF CLAVAMINATE SYNTHASE

1ds0, resolution 1.63Å

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