1dhp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:53, 7 February 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1dhp.gif|left|200px]]<br /><applet load="1dhp" size="350" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1dhp, resolution 2.3&Aring;" />
 
-
'''DIHYDRODIPICOLINATE SYNTHASE'''<br />
 
-
==Overview==
+
==DIHYDRODIPICOLINATE SYNTHASE==
-
The crystal structure of dihydrodipicolinate synthase from E. coli was, determined by multiple isomorphous replacement methods. The structure was, refined at a resolution of 2.5 A and the final R-factor is 19.6% for, 32,190 reflections between 10.0 A and 2.5 A and F &gt; 2 sigma (F). The, crystallographic asymmetric unit contains two monomers related by, approximate 2-fold symmetry. A tetramer with approximate 222 symmetry is, built up by crystallographic symmetry. The tetramer is almost planar with, no contacts between the subunits related by the non-crystallographic dyad., The active sites are accessible from a wide water-filled channel in the, center of the tetramer. The dihydrodipicolinate synthase monomer is, composed of two domains. Each polypeptide chain is folded into an 8-fold, alpha/beta barrel and a C-terminal alpha-helical domain comprising, residues 224 to 292. The fold is similar to that of N-acetylneuraminate, lyase. The active site lysine 161 is located in the alpha/beta barrel and, has access via two entrances from the C-terminal side of the barrel.
+
<StructureSection load='1dhp' size='340' side='right'caption='[[1dhp]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1dhp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DHP 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]] 2.3&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</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=1dhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dhp OCA], [https://pdbe.org/1dhp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dhp RCSB], [https://www.ebi.ac.uk/pdbsum/1dhp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dhp ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/DAPA_ECOLI DAPA_ECOLI] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).<ref>PMID:20503968</ref> <ref>PMID:8993314</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/dh/1dhp_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=1dhp ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1DHP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=K:'>K</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Dihydrodipicolinate_synthase Dihydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.52 4.2.1.52] Known structural/functional Site: <scene name='pdbsite=S1:Pyruvate+Binding+Residue'>S1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHP OCA].
+
*[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution., Mirwaldt C, Korndorfer I, Huber R, J Mol Biol. 1995 Feb 10;246(1):227-39. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7853400 7853400]
+
__TOC__
-
[[Category: Dihydrodipicolinate synthase]]
+
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Huber, R.]]
+
[[Category: Huber R]]
-
[[Category: Korndoerfer, I.]]
+
[[Category: Korndoerfer I]]
-
[[Category: Mirwaldt, C.]]
+
[[Category: Mirwaldt C]]
-
[[Category: K]]
+
-
[[Category: dihydrodipicolinate]]
+
-
[[Category: synthase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:35:30 2008''
+

Current revision

DIHYDRODIPICOLINATE SYNTHASE

PDB ID 1dhp

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dhp"
Personal tools