1jw0: Difference between revisions

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New page: left|200px<br /><applet load="1jw0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jw0, resolution 2.5Å" /> '''Structure of cephalos...
 
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[[Image:1jw0.gif|left|200px]]<br /><applet load="1jw0" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1jw0, resolution 2.5&Aring;" />
'''Structure of cephalosporin acylase in complex with glutarate'''<br />


==Overview==
==Structure of cephalosporin acylase in complex with glutarate==
BACKGROUND: Semisynthetic cephalosporins are primarily synthesized from, 7-aminocephalosporanic acid (7-ACA), which is obtained by environmentally, toxic chemical deacylation of cephalosporin C (CPC). Thus, the enzymatic, conversion of CPC to 7-ACA by cephalosporin acylase (CA) would be of great, interest. However, CAs use glutaryl-7-ACA (GL-7-ACA) as a primary, substrate and the enzyme has low turnover rates for CPC. RESULTS: The, binary complex structures of CA with GL-7-ACA and glutarate (the, side-chain of GL-7-ACA) show extensive interactions between the glutaryl, moiety of GL-7-ACA and the seven residues that form the side-chain pocket., These interactions explain why the D-alpha-aminoadipyl side-chain of CPC, yields a poorer substrate than GL-7-ACA. CONCLUSIONS: This understanding, of the nature of substrate specificity may be useful in the design of an, enzyme with an improved performance for the conversion of CPC to 7-ACA., Additionally, the catalytic mechanism of the deacylation reaction was, revealed by the ligand bound structures.
<StructureSection load='1jw0' size='340' side='right'caption='[[1jw0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jw0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevundimonas_diminuta Brevundimonas diminuta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JW0 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GUA:GLUTARIC+ACID'>GUA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1jw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jw0 OCA], [https://pdbe.org/1jw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jw0 RCSB], [https://www.ebi.ac.uk/pdbsum/1jw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jw0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G7AC_BREDI G7AC_BREDI] Catalyzes the deacylation of 7 beta-(4-carboxybutanamido)cephalosporanic acid (glutaryl-7-aminocephalosporanic acid or GL-7-ACA) to 7-aminocephalosporanic acid (7-ACA). Can not efficiently use cephalosporin C (CPC), penicillin G, or ampicillin as substrates.<ref>PMID:11080627</ref>
== 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/jw/1jw0_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=1jw0 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1JW0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Brevundimonas_diminuta Brevundimonas diminuta] with GUA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JW0 OCA].
*[[Cephalosporin acylase|Cephalosporin acylase]]
 
*[[Cephalosporin acylase 3D structures|Cephalosporin acylase 3D structures]]
==Reference==
== References ==
Structure of cephalosporin acylase in complex with glutaryl-7-aminocephalosporanic acid and glutarate: insight into the basis of its substrate specificity., Kim Y, Hol WG, Chem Biol. 2001 Dec;8(12):1253-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11755403 11755403]
<references/>
__TOC__
</StructureSection>
[[Category: Brevundimonas diminuta]]
[[Category: Brevundimonas diminuta]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Hol, W.G.J.]]
[[Category: Hol WGJ]]
[[Category: Kim, Y.]]
[[Category: Kim Y]]
[[Category: GUA]]
[[Category: cephalosporin acylase]]
[[Category: glutarate]]
[[Category: glutaryll-7-aca]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:37:30 2007''

Latest revision as of 10:55, 3 April 2024

Structure of cephalosporin acylase in complex with glutarateStructure of cephalosporin acylase in complex with glutarate

Structural highlights

1jw0 is a 2 chain structure with sequence from Brevundimonas diminuta. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

G7AC_BREDI Catalyzes the deacylation of 7 beta-(4-carboxybutanamido)cephalosporanic acid (glutaryl-7-aminocephalosporanic acid or GL-7-ACA) to 7-aminocephalosporanic acid (7-ACA). Can not efficiently use cephalosporin C (CPC), penicillin G, or ampicillin as substrates.[1]

Evolutionary Conservation

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

See Also

References

  1. ↑ Kim Y, Yoon K, Khang Y, Turley S, Hol WG. The 2.0 A crystal structure of cephalosporin acylase. Structure. 2000 Oct 15;8(10):1059-68. PMID:11080627

1jw0, resolution 2.50Å

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