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==Crystal Structure of O-actetyl Homoserine Sulfhydrylase From Thermus Thermophilus HB8,OAH2.==
==Crystal Structure of O-actetyl Homoserine Sulfhydrylase From Thermus Thermophilus HB8,OAH2.==
<StructureSection load='2cb1' size='340' side='right' caption='[[2cb1]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='2cb1' size='340' side='right'caption='[[2cb1]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2cb1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CB1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CB1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2cb1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CB1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CB1 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/O-acetylhomoserine_aminocarboxypropyltransferase O-acetylhomoserine aminocarboxypropyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.49 2.5.1.49] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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=2cb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cb1 OCA], [http://pdbe.org/2cb1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cb1 RCSB], [http://www.ebi.ac.uk/pdbsum/2cb1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cb1 ProSAT], [http://www.topsan.org/Proteins/RSGI/2cb1 TOPSAN]</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=2cb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cb1 OCA], [https://pdbe.org/2cb1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cb1 RCSB], [https://www.ebi.ac.uk/pdbsum/2cb1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cb1 ProSAT], [https://www.topsan.org/Proteins/RSGI/2cb1 TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/METY2_THET8 METY2_THET8] Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into homocysteine in the methionine biosynthesis pathway. Has weak activity with O-acetyl-L-serine, O-phospho-L-serine, L-serine, O-succinyl-L-homoserine and L-homoserine. Shows a very low CTT gamma-synthase activity.<ref>PMID:15215603</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=2cb1 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=2cb1 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: O-acetylhomoserine aminocarboxypropyltransferase]]
[[Category: Large Structures]]
[[Category: Thet8]]
[[Category: Thermus thermophilus HB8]]
[[Category: Agari, Y]]
[[Category: Agari Y]]
[[Category: Ebihara, A]]
[[Category: Ebihara A]]
[[Category: Imagawa, T]]
[[Category: Imagawa T]]
[[Category: Kanagawa, M]]
[[Category: Kanagawa M]]
[[Category: Kuramitsu, S]]
[[Category: Kuramitsu S]]
[[Category: Kuroishi, C]]
[[Category: Kuroishi C]]
[[Category: Nakagawa, N]]
[[Category: Nakagawa N]]
[[Category: Tsuge, H]]
[[Category: Tsuge H]]
[[Category: Utsunomiya, H]]
[[Category: Utsunomiya H]]
[[Category: Yokoyama, S]]
[[Category: Yokoyama S]]
[[Category: Homoserine]]
[[Category: Lyase]]
[[Category: Plp enzyme]]
[[Category: Structural genomic]]
[[Category: Rsgi]]
[[Category: Sulfhydrylase]]

Latest revision as of 17:11, 13 December 2023

Crystal Structure of O-actetyl Homoserine Sulfhydrylase From Thermus Thermophilus HB8,OAH2.Crystal Structure of O-actetyl Homoserine Sulfhydrylase From Thermus Thermophilus HB8,OAH2.

Structural highlights

2cb1 is a 1 chain structure with sequence from Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

METY2_THET8 Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into homocysteine in the methionine biosynthesis pathway. Has weak activity with O-acetyl-L-serine, O-phospho-L-serine, L-serine, O-succinyl-L-homoserine and L-homoserine. Shows a very low CTT gamma-synthase activity.[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. Iwama T, Hosokawa H, Lin W, Shimizu H, Kawai K, Yamagata S. Comparative characterization of the oah2 gene homologous to the oah1 of Thermus thermophilus HB8. Biosci Biotechnol Biochem. 2004 Jun;68(6):1357-61. PMID:15215603 doi:10.1271/bbb.68.1357

2cb1, resolution 2.00Å

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