1b9l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (23:21, 27 December 2023) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1b9l.png|left|200px]]
 
-
<!--
+
==7,8-DIHYDRONEOPTERIN TRIPHOSPHATE EPIMERASE==
-
The line below this paragraph, containing "STRUCTURE_1b9l", creates the "Structure Box" on the page.
+
<StructureSection load='1b9l' size='340' side='right'caption='[[1b9l]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1b9l]] is a 8 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=1B9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B9L FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</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=1b9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b9l OCA], [https://pdbe.org/1b9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b9l RCSB], [https://www.ebi.ac.uk/pdbsum/1b9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b9l ProSAT]</span></td></tr>
-
{{STRUCTURE_1b9l| PDB=1b9l | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/FOLX_ECOLI FOLX_ECOLI] Catalyzes the epimerization of carbon 2' of the side chain of dihydroneopterin triphosphate (H2NTP) to form dihydromonapterin triphosphate (H2MTP).
 +
== 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/b9/1b9l_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=1b9l ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
BACKGROUND: Dihydroneopterin triphosphate (H2NTP) is the central substrate in the biosynthesis of folate and tetrahydrobiopterin. Folate serves as a cofactor in amino acid and purine biosynthesis and tetrahydrobiopterin is used as a cofactor in amino acid hydroxylation and nitric oxide synthesis. In bacteria, H2NTP enters the folate biosynthetic pathway after nonenzymatic dephosphorylation; in vertebrates, H2NTP is used to synthesize tetrahydrobiopterin. The dihydroneopterin triphosphate epimerase of Escherichia coli catalyzes the inversion of carbon 2' of H2NTP. RESULTS: The crystal structure of the homo-octameric protein has been solved by a combination of multiple isomorphous replacement, Patterson search techniques and cyclic averaging and has been refined to a crystallographic R factor of 18.8% at 2.9 A resolution. The enzyme is a torus-shaped, D4 symmetric homo-octamer with approximate dimensions of 65 x 65 A. Four epimerase monomers form an unusual 16-stranded antiparallel beta barrel by tight association between the N- and C-terminal beta strands of two adjacent subunits. Two tetramers associate in a head-to-head fashion to form the active enzyme complex. CONCLUSIONS: The folding topology, quaternary structure and amino acid sequence of epimerase is similar to that of the dihydroneopterin aldolase involved in the biosynthesis of the vitamin folic acid. The monomer fold of epimerase is also topologically similar to that of GTP cyclohydrolase I (GTP CH-1), 6-pyrovoyl tetrahydropterin synthase (PTPS) and uroate oxidase (UO). Despite a lack of significant sequence homology these proteins share a common subunit fold and oligomerize to form central beta barrel structures employing different cyclic symmetry elements, D4, D5, D3 and D2, respectively. Moreover, these enzymes have a topologically equivalent acceptor site for the 2-amino-4-oxo pyrimidine (2-oxo-4-oxo pyrimidine in uroate oxidase) moiety of their respective substrates.
-
===7,8-DIHYDRONEOPTERIN TRIPHOSPHATE EPIMERASE===
+
Crystal structure of 7,8-dihydroneopterin triphosphate epimerase.,Ploom T, Haussmann C, Hof P, Steinbacher S, Bacher A, Richardson J, Huber R Structure. 1999 May;7(5):509-16. PMID:10378270<ref>PMID:10378270</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_10378270}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1b9l" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 10378270 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_10378270}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
1B9L is a 8 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B9L OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:10378270</ref><references group="xtra"/>
+
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Bacher, A.]]
+
[[Category: Large Structures]]
-
[[Category: Haussmann, C.]]
+
[[Category: Bacher A]]
-
[[Category: Hof, P.]]
+
[[Category: Haussmann C]]
-
[[Category: Huber, R.]]
+
[[Category: Hof P]]
-
[[Category: Ploom, T.]]
+
[[Category: Huber R]]
-
[[Category: Richardson, J.]]
+
[[Category: Ploom T]]
-
[[Category: Steinbacher, S.]]
+
[[Category: Richardson J]]
-
[[Category: Epimerase]]
+
[[Category: Steinbacher S]]
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 11:38:28 2009''
+

Current revision

7,8-DIHYDRONEOPTERIN TRIPHOSPHATE EPIMERASE

PDB ID 1b9l

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/1b9l"
Personal tools