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1sjc

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(New page: 200px<br /><applet load="1sjc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sjc, resolution 2.10&Aring;" /> '''x-ray structure of o...)
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[[Image:1sjc.gif|left|200px]]<br /><applet load="1sjc" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1sjc, resolution 2.10&Aring;" />
 
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'''x-ray structure of o-succinylbenzoate synthase complexed with N-succinyl methionine'''<br />
 
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==Overview==
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==x-ray structure of o-succinylbenzoate synthase complexed with N-succinyl methionine==
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Divergent evolution of enzyme function is commonly explained by a gene, duplication event followed by mutational changes that allow the protein, encoded by the copy to acquire a new function. An alternate hypothesis is, that this process is facilitated when the progenitor enzyme acquires a, second function while maintaining the original activity. This phenomenon, has been suggested to occur in the o-succinylbenzoate synthase (OSBS) from, a species of Amycolatopsis that catalyzes not only the physiological, syn-dehydration reaction of, 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate but also an, accidental racemization of N-acylamino acids [Palmer, D. R., Garrett, J., B., Sharma, V., Meganathan, R., Babbitt, P. C., and Gerlt, J. A. (1999), Biochemistry 38, 4252-4258]. To understand the molecular basis of this, promiscuity, three-dimensional structures of liganded complexes of this, enzyme have been determined, including the product of the OSBS reaction, and three N-acylamino acid substrates for the N-acylamino acid racemase, (NAAAR) reaction, N-acetylmethionine, N-succinylmethionine, and, N-succinylphenylglycine, to 2.2, 2.3, 2.1, and 1.9 A resolution, respectively. These structures show how the active-site cavity can, accommodate both the hydrophobic substrate for the OSBS reaction and the, substrates for the accidental NAAAR reaction. As expected, the N-acylamino, acid is sandwiched between lysines 163 and 263, which function as the, catalytic bases for the abstraction of the alpha-proton in the (R)- and, (S)-racemization reactions, respectively [Taylor Ringia, E. A., Garrett, J. B, Thoden, J. B., Holden, H. M., Rayment, I., and Gerlt, J. A. (2004), Biochemistry 42, 224-229]. Importantly, the protein forms specific, favorable interactions with the hydrophobic amino acid side chain, alpha-carbon, carboxylate, and the polar components of the N-acyl linkage., Accommodation of the components of the N-acyl linkage appears to be the, reason that this enzyme is capable of a racemization reaction on these, substrates, whereas the orthologous OSBS from Escherichia coli lacks this, functionality.
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<StructureSection load='1sjc' size='340' side='right'caption='[[1sjc]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1sjc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Amycolatopsis_sp. Amycolatopsis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SJC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SJC FirstGlance]. <br>
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1SJC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Amycolatopsis_sp. Amycolatopsis sp.] with MG and SMG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SJC OCA].
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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]] 2.1&#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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SMG:N-SUCCINYL+METHIONINE'>SMG</scene></td></tr>
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==Reference==
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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=1sjc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sjc OCA], [https://pdbe.org/1sjc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sjc RCSB], [https://www.ebi.ac.uk/pdbsum/1sjc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sjc ProSAT]</span></td></tr>
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Evolution of enzymatic activity in the enolase superfamily: structural studies of the promiscuous o-succinylbenzoate synthase from Amycolatopsis., Thoden JB, Taylor Ringia EA, Garrett JB, Gerlt JA, Holden HM, Rayment I, Biochemistry. 2004 May 18;43(19):5716-27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15134446 15134446]
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</table>
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[[Category: Amycolatopsis sp.]]
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== Function ==
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[[Category: Single protein]]
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[https://www.uniprot.org/uniprot/NSAR_AMYSP NSAR_AMYSP] Acts as a N-succinylamino acid racemase (NSAR) that catalyzes the racemization of N-succinyl-phenylglycine and N-succinyl-methionine (PubMed:14705949, PubMed:24955846). Can catalyze the racemization of a broad range of N-acylamino acids, including N-acetyl-D/L-methionine, N-propionyl-D/L-methionine, N-butyryl-D/L-methionine and N-chloroacetyl-L-valine (PubMed:7766084, PubMed:10194342, PubMed:14705949, PubMed:23130969). Also converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (PubMed:10194342, PubMed:14705949, PubMed:24955846). Catalyzes both N-succinylamino acid racemization and OSB synthesis at equivalent rates (PubMed:14705949, PubMed:24955846). NSAR is probably the biological function of this enzyme (Probable).<ref>PMID:10194342</ref> <ref>PMID:14705949</ref> <ref>PMID:23130969</ref> <ref>PMID:24955846</ref> <ref>PMID:7766084</ref> <ref>PMID:16740275</ref> <ref>PMID:24955846</ref>
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[[Category: Garrett, J.B.]]
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== Evolutionary Conservation ==
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[[Category: Gerlt, J.A.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Holden, H.M.]]
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Check<jmol>
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[[Category: Rayment, I.]]
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<jmolCheckbox>
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[[Category: Taylor-Ringia, E.A.]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sj/1sjc_consurf.spt"</scriptWhenChecked>
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[[Category: Thoden, J.B.]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: MG]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: SMG]]
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</jmolCheckbox>
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[[Category: racemase]]
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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=1sjc ConSurf].
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<div style="clear:both"></div>
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:37:37 2007''
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Amycolatopsis sp]]
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[[Category: Large Structures]]
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[[Category: Garrett JB]]
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[[Category: Gerlt JA]]
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[[Category: Holden HM]]
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[[Category: Rayment I]]
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[[Category: Taylor-Ringia EA]]
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[[Category: Thoden JB]]

Current revision

x-ray structure of o-succinylbenzoate synthase complexed with N-succinyl methionine

PDB ID 1sjc

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