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==Crystal structure of TTHA1623 in a di-iron-bound form== | |||
<StructureSection load='2zzi' size='340' side='right'caption='[[2zzi]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2zzi]] 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=2ZZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZZI 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]] 2.8Å</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=FE:FE+(III)+ION'>FE</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=2zzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zzi OCA], [https://pdbe.org/2zzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zzi RCSB], [https://www.ebi.ac.uk/pdbsum/2zzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zzi ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5SHV7_THET8 Q5SHV7_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/zz/2zzi_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=2zzi ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
TTHA1623 is a metallo-beta-lactamase superfamily protein from the extremely thermophilic bacterium Thermus thermophilus HB8. Homologues of TTHA1623 exist in a wide range of bacteria and archaea and one eukaryote, Giardia lamblia, but their function remains unknown. To analyze the structural properties of TTHA1623, the crystal structures of its iron-bound and zinc-bound forms have been determined to 2.8 and 2.2 A resolution, respectively. TTHA1623 possesses an alphabetabetaalpha-fold similar to that of other metallo-beta-lactamase superfamily proteins with glyoxalase II-type metal coordination. However, TTHA1623 exhibits a putative substrate-binding pocket with a unique shape. | |||
Structure of TTHA1623, a novel metallo-beta-lactamase superfamily protein from Thermus thermophilus HB8.,Yamamura A, Okada A, Kameda Y, Ohtsuka J, Nakagawa N, Ebihara A, Nagata K, Tanokura M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 May 1;65(Pt, 5):455-9. Epub 2009 Apr 24. PMID:19407375<ref>PMID:19407375</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2zzi" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermus thermophilus HB8]] | |||
[[Category: Ebihara A]] | |||
[[Category: Kameda Y]] | |||
[[Category: Kuramitsu S]] | |||
[[Category: Nagata K]] | |||
[[Category: Nakagawa N]] | |||
[[Category: Ohtsuka J]] | |||
[[Category: Okada A]] | |||
[[Category: Tanokura M]] | |||
[[Category: Yamamura A]] | |||
[[Category: Yokoyama S]] | |||
Latest revision as of 17:04, 1 November 2023
Crystal structure of TTHA1623 in a di-iron-bound formCrystal structure of TTHA1623 in a di-iron-bound form
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTTHA1623 is a metallo-beta-lactamase superfamily protein from the extremely thermophilic bacterium Thermus thermophilus HB8. Homologues of TTHA1623 exist in a wide range of bacteria and archaea and one eukaryote, Giardia lamblia, but their function remains unknown. To analyze the structural properties of TTHA1623, the crystal structures of its iron-bound and zinc-bound forms have been determined to 2.8 and 2.2 A resolution, respectively. TTHA1623 possesses an alphabetabetaalpha-fold similar to that of other metallo-beta-lactamase superfamily proteins with glyoxalase II-type metal coordination. However, TTHA1623 exhibits a putative substrate-binding pocket with a unique shape. Structure of TTHA1623, a novel metallo-beta-lactamase superfamily protein from Thermus thermophilus HB8.,Yamamura A, Okada A, Kameda Y, Ohtsuka J, Nakagawa N, Ebihara A, Nagata K, Tanokura M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 May 1;65(Pt, 5):455-9. Epub 2009 Apr 24. PMID:19407375[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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