1muc: Difference between revisions

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New page: left|200px<br /> <applet load="1muc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1muc, resolution 1.85Å" /> '''STRUCTURE OF MUCONA...
 
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[[Image:1muc.gif|left|200px]]<br />
<applet load="1muc" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1muc, resolution 1.85&Aring;" />
'''STRUCTURE OF MUCONATE LACTONIZING ENZYME AT 1.85 ANGSTROMS RESOLUTION'''<br />


==Overview==
==STRUCTURE OF MUCONATE LACTONIZING ENZYME AT 1.85 ANGSTROMS RESOLUTION==
We report here the refined X-ray crystal structure of muconate lactonizing, enzyme (MLE) from Pseudomonas putida PRS2000 at a resolution of 1.85 A, with an R-factor of 16.8%. An enzyme from the beta-ketoadipate pathway, MLE catalyses the conversion of cis,cis-muconate to muconolactone. It is a, homo-octamer, one monomer consisting of 373 amino acid residues. MLE has, two large domains and a C-terminal subdomain: an alpha + beta domain, an, alpha beta-barrel domain and a C-terminal meandering subdomain. The alpha, beta-barrel domain is highly irregular. Its structure is (beta/alpha)7, beta, with the structural role of the last alpha-helix being replaced by, both the C-terminal subdomain and part of the N-terminal domain. The, fifth, seventh and eighth barrel strands are unusual because ... [[http://ispc.weizmann.ac.il/pmbin/getpm?7500361 (full description)]]
<StructureSection load='1muc' size='340' side='right'caption='[[1muc]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1muc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1mle 1mle]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MUC 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]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=1muc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1muc OCA], [https://pdbe.org/1muc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1muc RCSB], [https://www.ebi.ac.uk/pdbsum/1muc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1muc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CATB_PSEPU CATB_PSEPU] Catalyzes a syn cycloisomerization.
== 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/mu/1muc_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=1muc ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1MUC is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]] with MN as [[http://en.wikipedia.org/wiki/ligand ligand]]. This structure superseeds the now removed PDB entry 1MLE. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.1 5.5.1.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MUC OCA]].
*[[Muconate cycloisomerase|Muconate cycloisomerase]]
 
__TOC__
==Reference==
</StructureSection>
The refined X-ray structure of muconate lactonizing enzyme from Pseudomonas putida PRS2000 at 1.85 A resolution., Helin S, Kahn PC, Guha BL, Mallows DG, Goldman A, J Mol Biol. 1995 Dec 15;254(5):918-41. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7500361 7500361]
[[Category: Large Structures]]
[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
[[Category: Single protein]]
[[Category: Goldman A]]
[[Category: Goldman, A.]]
[[Category: Guha BHL]]
[[Category: Guha, B.H.L.]]
[[Category: Helin S]]
[[Category: Helin, S.]]
[[Category: Kahn PC]]
[[Category: Kahn, P.C.]]
[[Category: Mallows DJ]]
[[Category: Mallows, D.J.]]
[[Category: MN]]
[[Category: muconate lactonizing enzyme]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 18:06:30 2007''

Latest revision as of 10:48, 14 February 2024

STRUCTURE OF MUCONATE LACTONIZING ENZYME AT 1.85 ANGSTROMS RESOLUTIONSTRUCTURE OF MUCONATE LACTONIZING ENZYME AT 1.85 ANGSTROMS RESOLUTION

Structural highlights

1muc is a 2 chain structure with sequence from Pseudomonas putida. This structure supersedes the now removed PDB entry 1mle. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.85Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CATB_PSEPU Catalyzes a syn cycloisomerization.

Evolutionary Conservation

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

See Also

1muc, resolution 1.85Å

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