1vm6: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(15 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1vm6.gif|left|200px]]<br /><applet load="1vm6" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1vm6, resolution 2.27&Aring;" />
'''Crystal structure of Dihydrodipicolinate reductase (TM1520) from Thermotoga maritima at 2.27 A resolution'''<br />


==About this Structure==
==Crystal structure of Dihydrodipicolinate reductase (TM1520) from Thermotoga maritima at 2.27 A resolution==
1VM6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=NAD:'>NAD</scene>, <scene name='pdbligand=EDO:'>EDO</scene> and <scene name='pdbligand=PG4:'>PG4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dihydrodipicolinate_reductase Dihydrodipicolinate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.26 1.3.1.26] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VM6 OCA].  
<StructureSection load='1vm6' size='340' side='right'caption='[[1vm6]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
[[Category: Dihydrodipicolinate reductase]]
== Structural highlights ==
[[Category: Single protein]]
<table><tr><td colspan='2'>[[1vm6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VM6 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]] 2.27&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=1vm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vm6 OCA], [https://pdbe.org/1vm6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vm6 RCSB], [https://www.ebi.ac.uk/pdbsum/1vm6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vm6 ProSAT], [https://www.topsan.org/Proteins/JCSG/1vm6 TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DAPB_THEMA DAPB_THEMA] Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate (Probable). Uses NADPH as a reductant with much more efficiency than NADH.<ref>PMID:18250105</ref>
== 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/vm/1vm6_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=1vm6 ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: JCSG, Joint Center for Structural Genomics.]]
[[Category: ACT]]
[[Category: EDO]]
[[Category: NAD]]
[[Category: PG4]]
[[Category: dihydrodipicolinate reductase]]
[[Category: jcsg]]
[[Category: joint center for structural genomics]]
[[Category: protein structure initiative]]
[[Category: psi]]
[[Category: structural genomics]]
[[Category: tm1520]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:36:46 2008''

Latest revision as of 17:53, 20 September 2023

Crystal structure of Dihydrodipicolinate reductase (TM1520) from Thermotoga maritima at 2.27 A resolutionCrystal structure of Dihydrodipicolinate reductase (TM1520) from Thermotoga maritima at 2.27 A resolution

Structural highlights

1vm6 is a 4 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.27Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

DAPB_THEMA Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate (Probable). Uses NADPH as a reductant with much more efficiency than NADH.[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. ↑ Pearce FG, Sprissler C, Gerrard JA. Characterization of dihydrodipicolinate reductase from Thermotoga maritima reveals evolution of substrate binding kinetics. J Biochem. 2008 May;143(5):617-23. doi: 10.1093/jb/mvn012. Epub 2008 Feb 4. PMID:18250105 doi:http://dx.doi.org/10.1093/jb/mvn012

1vm6, resolution 2.27Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1vm6&oldid=3874459"