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.


4q0p

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:51, 3 April 2024) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Crystal structure of Acinetobacter sp. DL28 L-ribose isomerase in complex with L-ribose==
==Crystal structure of Acinetobacter sp. DL28 L-ribose isomerase in complex with L-ribose==
-
<StructureSection load='4q0p' size='340' side='right' caption='[[4q0p]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
+
<StructureSection load='4q0p' size='340' side='right'caption='[[4q0p]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4q0p]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q0P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q0P FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4q0p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_sp._DL-28 Acinetobacter sp. DL-28]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q0P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q0P FirstGlance]. <br>
-
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0MK:L-RIBOPYRANOSE'>0MK</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=NCO:COBALT+HEXAMMINE(III)'>NCO</scene>, <scene name='pdbligand=Z6J:ALPHA-L-RIBOFURANOSE'>Z6J</scene><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]] 1.93&#8491;</td></tr>
-
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4q0q|4q0q]], [[4q0s|4q0s]], [[4q0u|4q0u]], [[4q0v|4q0v]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0MK:L-RIBOPYRANOSE'>0MK</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=NCO:COBALT+HEXAMMINE(III)'>NCO</scene>, <scene name='pdbligand=Z6J:ALPHA-L-RIBOFURANOSE'>Z6J</scene></td></tr>
-
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q0p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q0p RCSB], [http://www.ebi.ac.uk/pdbsum/4q0p PDBsum]</span></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=4q0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q0p OCA], [https://pdbe.org/4q0p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q0p RCSB], [https://www.ebi.ac.uk/pdbsum/4q0p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q0p ProSAT]</span></td></tr>
-
<table>
+
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/Q93UQ5_9GAMM Q93UQ5_9GAMM]
-
Acinetobacter sp. L-ribose isomerase (L-RI) catalyzes a reversible isomerization reaction between L-ribose and L-ribulose. To date, information on L-RI remains limited and its amino-acid sequence shows no similarity to those of any known enzymes. Here, recombinant His-tagged L-RI was successfully overexpressed, purified and crystallized. Crystals of His-tagged L-RI were obtained by the hanging-drop vapour-diffusion method at room temperature as two crystal forms which belonged to the monoclinic space group C2, with unit-cell parameters a = 96.60, b = 105.89, c = 71.83 A, beta = 118.16 degrees , and the orthorhombic space group F222, with unit-cell parameters a = 96.44, b = 106.26, c = 117.83 A. Diffraction data were collected to 3.1 and 2.2 A resolution, respectively.
+
-
 
+
-
Overexpression, crystallization and preliminary X-ray diffraction analysis of L-ribose isomerase from Acinetobacter sp. strain DL-28.,Yoshida H, Teraoka M, Yoshihara A, Izumori K, Kamitori S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Oct 1;67(Pt 10):1281-4., doi: 10.1107/S1744309111030351. Epub 2011 Sep 30. PMID:22102048<ref>PMID:22102048</ref>
+
-
 
+
-
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Izumori, K.]]
+
[[Category: Acinetobacter sp. DL-28]]
-
[[Category: Kamitori, S.]]
+
[[Category: Large Structures]]
-
[[Category: Teraoka, M.]]
+
[[Category: Izumori K]]
-
[[Category: Yoshida, H.]]
+
[[Category: Kamitori S]]
-
[[Category: Yoshihara, A.]]
+
[[Category: Teraoka M]]
-
[[Category: Cupin barrel]]
+
[[Category: Yoshida H]]
-
[[Category: Isomerase]]
+
[[Category: Yoshihara A]]
-
[[Category: Sugar binding]]
+

Current revision

Crystal structure of Acinetobacter sp. DL28 L-ribose isomerase in complex with L-ribose

PDB ID 4q0p

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools