1vrq: Difference between revisions

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<StructureSection load='1vrq' size='340' side='right'caption='[[1vrq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1vrq' size='340' side='right'caption='[[1vrq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1vrq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_u-96 Corynebacterium u-96]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VRQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[1vrq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_sp._U-96 Corynebacterium sp. U-96]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VRQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMG:N,N-DIMETHYLGLYCINE'>DMG</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=FON:N-{[4-({[(6R)-2-AMINO-5-FORMYL-4-OXO-1,4,5,6,7,8-HEXAHYDROPTERIDIN-6-YL]METHYL}AMINO)PHENYL]CARBONYL}-L-GLUTAMIC+ACID'>FON</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1l9f|1l9f]], [[1el5|1el5]], [[1pj5|1pj5]], [[1pj6|1pj6]], [[1pj7|1pj7]], [[1woo|1woo]], [[1x31|1x31]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMG:N,N-DIMETHYLGLYCINE'>DMG</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=FON:N-{[4-({[(6R)-2-AMINO-5-FORMYL-4-OXO-1,4,5,6,7,8-HEXAHYDROPTERIDIN-6-YL]METHYL}AMINO)PHENYL]CARBONYL}-L-GLUTAMIC+ACID'>FON</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Sarcosine_oxidase Sarcosine oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.1 1.5.3.1] </span></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=1vrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vrq OCA], [https://pdbe.org/1vrq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vrq RCSB], [https://www.ebi.ac.uk/pdbsum/1vrq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vrq ProSAT]</span></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=1vrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vrq OCA], [https://pdbe.org/1vrq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vrq RCSB], [https://www.ebi.ac.uk/pdbsum/1vrq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vrq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q50LF1_9CORY Q50LF1_9CORY]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Corynebacterium u-96]]
[[Category: Corynebacterium sp. U-96]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Sarcosine oxidase]]
[[Category: Ida K]]
[[Category: Ida, K]]
[[Category: Moriguchi T]]
[[Category: Moriguchi, T]]
[[Category: Suzuki H]]
[[Category: Suzuki, H]]
[[Category: Flavoenzyme]]
[[Category: Heterotetrameric sarcosine oxidase]]
[[Category: Oxidoreductase]]

Latest revision as of 03:05, 28 December 2023

Crystal Structure of Heterotetrameric Sarcosine Oxidase from Corynebacterium sp. U-96 in complex with Folinic AcidCrystal Structure of Heterotetrameric Sarcosine Oxidase from Corynebacterium sp. U-96 in complex with Folinic Acid

Structural highlights

1vrq is a 4 chain structure with sequence from Corynebacterium sp. U-96. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:, , , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q50LF1_9CORY

Evolutionary Conservation

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

Publication Abstract from PubMed

Sarcosine oxidase from Corynebacterium sp. U-96 is a heterotetrameric enzyme. Here we report the crystal structures of the enzyme in complex with dimethylglycine and folinic acid. The alpha subunit is composed of two domains, contains NAD(+), and binds folinic acid. The beta subunit contains dimethylglycine, FAD, and FMN, and these flavins are approximately 10A apart. The gamma subunit is in contact with two domains of alpha subunit and has possibly a folate-binding structure. The delta subunit contains a single atom of zinc and has a Cys(3)His zinc finger structure. Based on the structures determined and on the previous works, the structure-function relationship on the heterotetrameric sarcosine oxidase is discussed.

Crystal structure of heterotetrameric sarcosine oxidase from Corynebacterium sp. U-96.,Ida K, Moriguchi T, Suzuki H Biochem Biophys Res Commun. 2005 Jul 29;333(2):359-66. PMID:15946648[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Ida K, Moriguchi T, Suzuki H. Crystal structure of heterotetrameric sarcosine oxidase from Corynebacterium sp. U-96. Biochem Biophys Res Commun. 2005 Jul 29;333(2):359-66. PMID:15946648 doi:10.1016/j.bbrc.2005.05.116

1vrq, resolution 2.20Å

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