This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1k75

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1k75" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k75, resolution 1.75&Aring;" /> '''The L-histidinol deh...)
Current revision (07:58, 3 April 2024) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1k75.jpg|left|200px]]<br /><applet load="1k75" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1k75, resolution 1.75&Aring;" />
 
-
'''The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.'''<br />
 
-
==Overview==
+
==The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.==
-
The histidine biosynthetic pathway is an ancient one found in bacteria, archaebacteria, fungi, and plants that converts 5-phosphoribosyl, 1-pyrophosphate to l-histidine in 10 enzymatic reactions. This pathway, provided a paradigm for the operon, transcriptional regulation of gene, expression, and feedback inhibition of a pathway. l-histidinol, dehydrogenase (HisD, EC ) catalyzes the last two steps in the biosynthesis, of l-histidine: sequential NAD-dependent oxidations of l-histidinol to, l-histidinaldehyde and then to l-histidine. HisD functions as a homodimer, and requires the presence of one Zn(2+) cation per monomer. We have, determined the three-dimensional structure of Escherichia coli HisD in the, apo state as well as complexes with substrate, Zn(2+), and NAD(+) (best, resolution is 1.7 A). Each monomer is made of four domains, whereas the, intertwined dimer possibly results from domain swapping. Two domains, display a very similar incomplete Rossmann fold that suggests an ancient, event of gene duplication. Residues from both monomers form the active, site. Zn(2+) plays a crucial role in substrate binding but is not directly, involved in catalysis. The active site residue His-327 participates in, acid-base catalysis, whereas Glu-326 activates a water molecule. NAD(+), binds weakly to one of the Rossmann fold domains in a manner different, from that previously observed for other proteins having a Rossmann fold.
+
<StructureSection load='1k75' size='340' side='right'caption='[[1k75]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<table><tr><td colspan='2'>[[1k75]] 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=1K75 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K75 FirstGlance]. <br>
-
1K75 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 SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Histidinol_dehydrogenase Histidinol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.23 1.1.1.23] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K75 OCA].
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
-
 
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
==Reference==
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k75 OCA], [https://pdbe.org/1k75 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k75 RCSB], [https://www.ebi.ac.uk/pdbsum/1k75 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k75 ProSAT], [https://www.topsan.org/Proteins/BSGI/1k75 TOPSAN]</span></td></tr>
-
Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase., Barbosa JA, Sivaraman J, Li Y, Larocque R, Matte A, Schrag JD, Cygler M, Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1859-64. Epub 2002 Feb 12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11842181 11842181]
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/HISX_ECOLI HISX_ECOLI] Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.[HAMAP-Rule:MF_01024]
 +
== 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/k7/1k75_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=1k75 ConSurf].
 +
<div style="clear:both"></div>
 +
__TOC__
 +
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Histidinol dehydrogenase]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Barbosa JARG]]
-
[[Category: BSGI, Montreal-Kingston.Bacterial.Structural.Genomics.Initiative.]]
+
[[Category: Cygler M]]
-
[[Category: Barbosa, J.A.R.G.]]
+
[[Category: Larocque R]]
-
[[Category: Cygler, M.]]
+
[[Category: Li Y]]
-
[[Category: Larocque, R.]]
+
[[Category: Matte A]]
-
[[Category: Li, Y.]]
+
[[Category: Schrag J]]
-
[[Category: Matte, A.]]
+
[[Category: Sivaraman J]]
-
[[Category: Schrag, J.]]
+
-
[[Category: Sivaraman, J.]]
+
-
[[Category: GOL]]
+
-
[[Category: SO4]]
+
-
[[Category: 4 domains]]
+
-
[[Category: bsgi]]
+
-
[[Category: hisd]]
+
-
[[Category: homodimer]]
+
-
[[Category: l-histidine biosynthesis]]
+
-
[[Category: l-histidinol dehydrogenase]]
+
-
[[Category: montreal-kingston bacterial structural genomics initiative]]
+
-
[[Category: nad cofactor]]
+
-
[[Category: rossman fold]]
+
-
[[Category: structural genomics]]
+
-
[[Category: zinc]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:54:32 2007''
+

Current revision

The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.

PDB ID 1k75

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/1k75"
Personal tools