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==The crystal structure of an amidohydrolase from Mycoplasma synoviae==
==The crystal structure of an amidohydrolase from Mycoplasma synoviae==
<StructureSection load='3msr' size='340' side='right' caption='[[3msr]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
<StructureSection load='3msr' size='340' side='right'caption='[[3msr]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3msr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycs5 Mycs5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MSR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MSR FirstGlance]. <br>
<table><tr><td colspan='2'>[[3msr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycoplasmopsis_synoviae_53 Mycoplasmopsis synoviae 53]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MSR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MSR FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.162&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HAD, MS53_0025 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262723 MYCS5])</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=3msr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3msr OCA], [https://pdbe.org/3msr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3msr RCSB], [https://www.ebi.ac.uk/pdbsum/3msr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3msr ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3msr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3msr OCA], [http://pdbe.org/3msr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3msr RCSB], [http://www.ebi.ac.uk/pdbsum/3msr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3msr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PFLAC_MYCS5 PFLAC_MYCS5] Catalyzes the hydrolysis of D-xylono-1,4-lactone-5-phosphate and L-arabino-1,4-lactone-5-phosphate. Also able to hydrolyze carboxy 1,4-lactones.<ref>PMID:24955762</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ms/3msr_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ms/3msr_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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=3msr ConSurf].
</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=3msr ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Mycs5]]
[[Category: Large Structures]]
[[Category: Burley, S K]]
[[Category: Mycoplasmopsis synoviae 53]]
[[Category: Structural genomic]]
[[Category: Burley SK]]
[[Category: Swaminathan, S]]
[[Category: Swaminathan S]]
[[Category: Zhang, Z]]
[[Category: Zhang Z]]
[[Category: Amidohydrolase]]
[[Category: Had]]
[[Category: Hydrolase]]
[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
[[Category: PSI, Protein structure initiative]]
[[Category: Sgx]]

Latest revision as of 09:30, 27 November 2024

The crystal structure of an amidohydrolase from Mycoplasma synoviaeThe crystal structure of an amidohydrolase from Mycoplasma synoviae

Structural highlights

3msr is a 1 chain structure with sequence from Mycoplasmopsis synoviae 53. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.162Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PFLAC_MYCS5 Catalyzes the hydrolysis of D-xylono-1,4-lactone-5-phosphate and L-arabino-1,4-lactone-5-phosphate. Also able to hydrolyze carboxy 1,4-lactones.[1]

Evolutionary Conservation

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

References

  1. ↑ Korczynska M, Xiang DF, Zhang Z, Xu C, Narindoshvili T, Kamat SS, Williams HJ, Chang SS, Kolb P, Hillerich B, Sauder JM, Burley SK, Almo SC, Swaminathan S, Shoichet BK, Raushel FM. Functional annotation and structural characterization of a novel lactonase hydrolyzing D-xylono-1,4-lactone-5-phosphate and L-arabino-1,4-lactone-5-phosphate. Biochemistry. 2014 Jul 22;53(28):4727-38. PMID:24955762 doi:10.1021/bi500595c

3msr, resolution 2.16Å

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