1ahh: Difference between revisions

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New page: left|200px<br /><applet load="1ahh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ahh, resolution 2.3Å" /> '''7 ALPHA-HYDROXYSTEROI...
 
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[[Image:1ahh.gif|left|200px]]<br /><applet load="1ahh" size="450" color="white" frame="true" align="right" spinBox="true"
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'''7 ALPHA-HYDROXYSTEROID DEHYDROGENASE COMPLEXED WITH NAD+'''<br />


==Overview==
==7 ALPHA-HYDROXYSTEROID DEHYDROGENASE COMPLEXED WITH NAD+==
7 alpha-Hydroxysteroid dehydrogenase (7 alpha-HSDH;1 EC 1.1.1.159) is an, NAD+-dependent oxidoreductase belonging to the short-chain, dehydrogenase/reductase (SDR) 1 family. It catalyzes the dehydrogenation, of a hydroxyl group at position 7 of the steroid skeleton of bile acids., The crystal structure of the binary (complexed with NAD+) complex of 7, alpha-HSDH has been solved at 2.3 A resolution by the multiple isomorphous, replacement method. The structure of the ternary complex [the enzyme, complexed with NADH, 7-oxoglycochenodeoxycholic acid (as a reaction, product), and possibly partially glycochenodeoxycholic acid (as a, substrate)] has been determined by a difference Fourier method at 1.8 A, resolution. The enzyme 7 alpha-HSDH is an alpha/beta doubly wound protein, having a Rossmann-fold domain for NAD (H) binding. Upon substrate binding, large conformation changes occur at the substrate binding loop (between, the beta F strand and alpha G helix) and the C-terminal segment (residues, 250-255). The variable amino acid sequences of the substrate-binding loop, appear to be responsible for the wide variety of substrate specificities, observed among the enzymes of the SDR family. The crystal structure of the, ternary complex of 7 alpha-HSDH, which is the only structure available as, the ternary complex among the enzymes of the SDR family, indicates that, the highly conserved Tyr159 and Ser146 residues most probably directly, interact with the hydroxyl group of the substrates although this, observation cannot be definite due to an insufficiently characterized, nature of the ternary complex. The strictly conserved Lys163 is, hydrogen-bonded to both the 2'- and 3'-hydroxyl groups of the nicotinamide, ribose of NAD(H). We propose a new catalytic mechanism possibly common to, all the enzymes belonging to the SDR family in which a tyrosine residue, (Tyr159) acts as a catalytic base and a serine residue (Ser146) plays a, subsidiary role of stabilizing substrate binding.
<StructureSection load='1ahh' size='340' side='right'caption='[[1ahh]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ahh]] 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=1AHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AHH 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=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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=1ahh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ahh OCA], [https://pdbe.org/1ahh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ahh RCSB], [https://www.ebi.ac.uk/pdbsum/1ahh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ahh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HDHA_ECOLI HDHA_ECOLI] 7-alpha-dehydroxylation of cholic acid, yielding deoxycholic acid and lithocholic acid, respectively. Highest affinity with taurochenodeoxycholic acid.
== 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/ah/1ahh_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=1ahh ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1AHH 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 NAD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/7-alpha-hydroxysteroid_dehydrogenase 7-alpha-hydroxysteroid dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.159 1.1.1.159] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AHH OCA].
*[[Hydroxysteroid dehydrogenase 3D structures|Hydroxysteroid dehydrogenase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structures of the binary and ternary complexes of 7 alpha-hydroxysteroid dehydrogenase from Escherichia coli., Tanaka N, Nonaka T, Tanabe T, Yoshimoto T, Tsuru D, Mitsui Y, Biochemistry. 1996 Jun 18;35(24):7715-30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8672472 8672472]
[[Category: 7-alpha-hydroxysteroid dehydrogenase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Mitsui, Y.]]
[[Category: Mitsui Y]]
[[Category: Nonaka, T.]]
[[Category: Nonaka T]]
[[Category: Tanaka, N.]]
[[Category: Tanaka N]]
[[Category: NAD]]
[[Category: colon bacillus]]
[[Category: oxidoreductase]]
[[Category: short-chain dehydrogenase/reductase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:51:31 2007''

Latest revision as of 09:30, 7 February 2024

7 ALPHA-HYDROXYSTEROID DEHYDROGENASE COMPLEXED WITH NAD+7 ALPHA-HYDROXYSTEROID DEHYDROGENASE COMPLEXED WITH NAD+

Structural highlights

1ahh is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HDHA_ECOLI 7-alpha-dehydroxylation of cholic acid, yielding deoxycholic acid and lithocholic acid, respectively. Highest affinity with taurochenodeoxycholic acid.

Evolutionary Conservation

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

See Also

1ahh, resolution 2.30Å

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