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1muc

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[[Image:1muc.gif|left|200px]]<br /><applet load="1muc" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1muc, resolution 1.85&Aring;" />
 
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'''STRUCTURE OF MUCONATE LACTONIZING ENZYME AT 1.85 ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==STRUCTURE OF MUCONATE LACTONIZING ENZYME AT 1.85 ANGSTROMS RESOLUTION==
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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 they have, left-handed twist about their axes. The strand crossing angles also vary, enormously, from +9 degrees to -69 degrees; the first and last strands, which close the barrel, cross at an angle of -69 degrees, making extensive, strand-strand hydrogen bonding impossible. The first barrel strand is also, unusual because it starts in the N-terminal domain and forms hydrogen, bonds to the C-terminal subdomain beta-sheet as well as to its, neighbouring strands in the barrel. It thus cements the whole protein, together. As in other alpha beta-barrel proteins, the active site of MLE, present in each subunit is at the C-terminal ends of the barrel, beta-strands. The active site cleft contains an essential manganese ion, is lined with charged and other polar residues, and contains many of the, crystallographic water molecules. The manganese ion is octahedrally, co-ordinated to three side-chain carboxylate groups and three water, molecules, and is at the centre of a radiating web of ionic and, hydrogen-bonding interactions. Additionally, two water molecules are, buried in the centre of the barrel and two hydrophilic side-chains (Lys167, and Arg196) make both hydrophobic and hydrophilic packing interactions, with much of the barrel interior. The barrel interior is thus also unusual, because it is so hydrophilic; the dominating force appears to be the need, to solvate the metal ion effectively. This might account for the, irregularity of the barrel. The catalytic mechanism has been investigated, by docking both substrate and product in the active site with the C-COO-, of muconolactone superimposed on the corresponding atoms of, cis,cis-muconate. In agreement with earlier kinetic and spectroscopic, results, the manganese ion does not interact directly with substrate or, product.(ABSTRACT TRUNCATED AT 400 WORDS)
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<StructureSection load='1muc' size='340' side='right'caption='[[1muc]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CATB_PSEPU CATB_PSEPU] Catalyzes a syn cycloisomerization.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mu/1muc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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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/Muconate_cycloisomerase Muconate cycloisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.1 5.5.1.1] Known structural/functional Sites: <scene name='pdbsite=MNA:Residues Involved In The Coordination Of Mn-Ion In Chain A'>MNA</scene> and <scene name='pdbsite=MNB:Residues Involved In The Coordination Of Mn-Ion In Chain'>MNB</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MUC OCA].
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*[[Muconate cycloisomerase|Muconate cycloisomerase]]
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__TOC__
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==Reference==
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</StructureSection>
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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]
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[[Category: Large Structures]]
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[[Category: Muconate cycloisomerase]]
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[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
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[[Category: Single protein]]
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[[Category: Goldman A]]
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[[Category: Goldman, A.]]
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[[Category: Guha BHL]]
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[[Category: Guha, B.H.L.]]
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[[Category: Helin S]]
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[[Category: Helin, S.]]
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[[Category: Kahn PC]]
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[[Category: Kahn, P.C.]]
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[[Category: Mallows DJ]]
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[[Category: Mallows, D.J.]]
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[[Category: MN]]
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[[Category: muconate lactonizing enzyme]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 16:46:46 2007''
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Current revision

STRUCTURE OF MUCONATE LACTONIZING ENZYME AT 1.85 ANGSTROMS RESOLUTION

PDB ID 1muc

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