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[[Image:2bhq.gif|left|200px]]<br />
<applet load="2bhq" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2bhq, resolution 1.40&Aring;" />
'''CRYSTAL ANALYSIS OF 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE FROM THERMUS WITH BOUND PRODUCT GLUTAMATE.'''<br />


==Overview==
==Crystal Analysis of 1-Pyrroline-5-Carboxylate Dehydrogenase from Thermus with bound product glutamate.==
Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDh) plays an important, role in the metabolic pathway from proline to glutamate. It irreversibly, catalyzes the oxidation of glutamate-gamma-semialdehyde, the product of, the non-enzymatic hydrolysis of Delta(1)-pyrroline-5-carboxylate, into, glutamate with the reduction of NAD(+) into NADH. We have confirmed the, P5CDh activity of the Thermus thermophilus protein TT0033 (TtP5CDh), and, determined the crystal structure of the enzyme in the ligand-free form at, 1.4 A resolution. To investigate the structural basis of TtP5CDh function, the TtP5CDh structures with NAD(+), with NADH, and with its product, glutamate were determined at 1.8 A, 1.9 A, and 1.4 A resolution, respectively. The solved structures suggest an overall view of the P5CDh, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?16934832 (full description)]]
<StructureSection load='2bhq' size='340' side='right'caption='[[2bhq]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2bhq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BHQ 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]] 1.4&#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=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</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=2bhq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bhq OCA], [https://pdbe.org/2bhq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bhq RCSB], [https://www.ebi.ac.uk/pdbsum/2bhq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bhq ProSAT], [https://www.topsan.org/Proteins/RSGI/2bhq TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5SI02_THET8 Q5SI02_THET8]
== 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/bh/2bhq_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=2bhq ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDh) plays an important role in the metabolic pathway from proline to glutamate. It irreversibly catalyzes the oxidation of glutamate-gamma-semialdehyde, the product of the non-enzymatic hydrolysis of Delta(1)-pyrroline-5-carboxylate, into glutamate with the reduction of NAD(+) into NADH. We have confirmed the P5CDh activity of the Thermus thermophilus protein TT0033 (TtP5CDh), and determined the crystal structure of the enzyme in the ligand-free form at 1.4 A resolution. To investigate the structural basis of TtP5CDh function, the TtP5CDh structures with NAD(+), with NADH, and with its product glutamate were determined at 1.8 A, 1.9 A, and 1.4 A resolution, respectively. The solved structures suggest an overall view of the P5CDh catalytic mechanism and provide insights into the P5CDh deficiencies in the case of the human type II hyperprolinemia.


==About this Structure==
Crystal structure of Thermus thermophilus Delta1-pyrroline-5-carboxylate dehydrogenase.,Inagaki E, Ohshima N, Takahashi H, Kuroishi C, Yokoyama S, Tahirov TH J Mol Biol. 2006 Sep 22;362(3):490-501. Epub 2006 Jul 29. PMID:16934832<ref>PMID:16934832</ref>
2BHQ is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]] with ACT, GLU, MRD and MPD as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/1-pyrroline-5-carboxylate_dehydrogenase 1-pyrroline-5-carboxylate dehydrogenase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.12 1.5.1.12]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BHQ OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of Thermus thermophilus Delta1-pyrroline-5-carboxylate dehydrogenase., Inagaki E, Ohshima N, Takahashi H, Kuroishi C, Yokoyama S, Tahirov TH, J Mol Biol. 2006 Sep 22;362(3):490-501. Epub 2006 Jul 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16934832 16934832]
</div>
[[Category: 1-pyrroline-5-carboxylate dehydrogenase]]
<div class="pdbe-citations 2bhq" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
[[Category: Thermus thermophilus]]
[[Category: Inagaki, E.]]
[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
[[Category: Tahirov, T.H.]]
[[Category: ACT]]
[[Category: GLU]]
[[Category: MPD]]
[[Category: MRD]]
[[Category: 1-pyrroline-5-carboxylate]]
[[Category: dehyrogenase]]
[[Category: oxidoreductase]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: structural genomics]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:38:09 2007''
==See Also==
*[[Pyrroline-5-carboxylate dehydrogenase|Pyrroline-5-carboxylate dehydrogenase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus thermophilus HB8]]
[[Category: Inagaki E]]
[[Category: Tahirov TH]]

Latest revision as of 16:38, 13 December 2023

Crystal Analysis of 1-Pyrroline-5-Carboxylate Dehydrogenase from Thermus with bound product glutamate.Crystal Analysis of 1-Pyrroline-5-Carboxylate Dehydrogenase from Thermus with bound product glutamate.

Structural highlights

2bhq is a 2 chain structure with sequence from Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.4Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

Q5SI02_THET8

Evolutionary Conservation

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

Publication Abstract from PubMed

Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDh) plays an important role in the metabolic pathway from proline to glutamate. It irreversibly catalyzes the oxidation of glutamate-gamma-semialdehyde, the product of the non-enzymatic hydrolysis of Delta(1)-pyrroline-5-carboxylate, into glutamate with the reduction of NAD(+) into NADH. We have confirmed the P5CDh activity of the Thermus thermophilus protein TT0033 (TtP5CDh), and determined the crystal structure of the enzyme in the ligand-free form at 1.4 A resolution. To investigate the structural basis of TtP5CDh function, the TtP5CDh structures with NAD(+), with NADH, and with its product glutamate were determined at 1.8 A, 1.9 A, and 1.4 A resolution, respectively. The solved structures suggest an overall view of the P5CDh catalytic mechanism and provide insights into the P5CDh deficiencies in the case of the human type II hyperprolinemia.

Crystal structure of Thermus thermophilus Delta1-pyrroline-5-carboxylate dehydrogenase.,Inagaki E, Ohshima N, Takahashi H, Kuroishi C, Yokoyama S, Tahirov TH J Mol Biol. 2006 Sep 22;362(3):490-501. Epub 2006 Jul 29. PMID:16934832[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Inagaki E, Ohshima N, Takahashi H, Kuroishi C, Yokoyama S, Tahirov TH. Crystal structure of Thermus thermophilus Delta1-pyrroline-5-carboxylate dehydrogenase. J Mol Biol. 2006 Sep 22;362(3):490-501. Epub 2006 Jul 29. PMID:16934832 doi:http://dx.doi.org/10.1016/j.jmb.2006.07.048

2bhq, resolution 1.40Å

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