2vi9: Difference between revisions

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[[Image:2vi9.jpg|left|200px]]<br /><applet load="2vi9" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2vi9, resolution 2.00&Aring;" />
'''CRYSTAL STRUCTURE OF S172ABSSHMT GLYCINE EXTERNAL ALDIMINE'''<br />


==About this Structure==
==Crystal structure of S172AbsSHMT Glycine external aldimine==
2VI9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=GLY:'>GLY</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1] Known structural/functional Sites: <scene name='pdbsite=AC1:Plp+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:GLY+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Mpd+Binding+Site+For+Chain+A'>AC3</scene> and <scene name='pdbsite=AC4:Mpd+Binding+Site+For+Chain+A'>AC4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VI9 OCA].  
<StructureSection load='2vi9' size='340' side='right'caption='[[2vi9]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2vi9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VI9 FirstGlance]. <br>
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=2vi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vi9 OCA], [https://pdbe.org/2vi9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vi9 RCSB], [https://www.ebi.ac.uk/pdbsum/2vi9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vi9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q7SIB6_GEOSE Q7SIB6_GEOSE] Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.[HAMAP-Rule:MF_00051]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vi/2vi9_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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=2vi9 ConSurf].
<div style="clear:both"></div>
 
==See Also==
*[[Serine hydroxymethyltransferase 3D structures|Serine hydroxymethyltransferase 3D structures]]
__TOC__
</StructureSection>
[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Glycine hydroxymethyltransferase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Appaji Rao N]]
[[Category: Bhavani, B S.]]
[[Category: Bhavani BS]]
[[Category: Murthy, M R.N.]]
[[Category: Murthy MRN]]
[[Category: Prakash, V.]]
[[Category: Prakash V]]
[[Category: Rajaram, V.]]
[[Category: Rajaram V]]
[[Category: Rao, N Appaji.]]
[[Category: Savithri HS]]
[[Category: Savithri, H S.]]
[[Category: GLY]]
[[Category: MPD]]
[[Category: PO4]]
[[Category: e53q]]
[[Category: enzyme memory]]
[[Category: fthf]]
[[Category: one-carbon metabolism]]
[[Category: plp-dependent enzymes]]
[[Category: pyridoxal phosphate]]
[[Category: shmt]]
[[Category: transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:56:02 2008''

Latest revision as of 18:21, 13 December 2023

Crystal structure of S172AbsSHMT Glycine external aldimineCrystal structure of S172AbsSHMT Glycine external aldimine

Structural highlights

2vi9 is a 1 chain structure with sequence from Geobacillus stearothermophilus. 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

Function

Q7SIB6_GEOSE Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.[HAMAP-Rule:MF_00051]

Evolutionary Conservation

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

See Also

2vi9, resolution 2.00Å

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