1oz9: Difference between revisions

Revision as of 15:52, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1oz9.png

Template:STRUCTURE 1oz9

Crystal structure of AQ_1354, a hypothetical protein from Aquifex aeolicusCrystal structure of AQ_1354, a hypothetical protein from Aquifex aeolicus

Template:ABSTRACT PUBMED 12832766

About this StructureAbout this Structure

1OZ9 is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the hypothetical protein AQ_1354 from Aquifex aeolicus., Oganesyan V, Busso D, Brandsen J, Chen S, Jancarik J, Kim R, Kim SH, Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1219-23. Epub 2003, Jun 27. PMID:12832766

Page seeded by OCA on Sun Jul 27 15:52:12 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1oz9.gif|left|200px]]
+{{Seed}}
+[[Image:1oz9.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1oz9|  PDB=1oz9  |  SCENE=  }}
-'''Crystal structure of AQ_1354, a hypothetical protein from Aquifex aeolicus'''
+===Crystal structure of AQ_1354, a hypothetical protein from Aquifex aeolicus===
-==Overview==
+<!--
-The crystal structure of a hypothetical protein AQ_1354 (gi 2983779) from the hyperthermophilic bacteria Aquifex aeolicus has been determined using X-ray crystallography. As found in many structural genomics studies, this protein is not associated with any known function based on its amino-acid sequence. PSI-BLAST analysis against a non-redundant sequence database gave 68 similar sequences referred to as 'conserved hypothetical proteins' from the uncharacterized protein family UPF0054 (accession No. PF02310). Crystallographic analysis revealed that the overall fold of this protein consists of one central alpha-helix surrounded by a four-stranded beta-sheet and four other alpha-helices. Structure-based homology analysis with DALI revealed that the structure has a moderate to good resemblance to metal-dependent proteinases such as collagenases and gelatinases, thus suggesting its possible molecular function. However, experimental tests for collagenase and gelatinase-type function show no detectable activity under standard assay conditions. Therefore, we suggest either that the members of the UPF0054 family have a similar fold but different biochemical functions to those of collagenases and gelatinases or that they have a similar function but perform it under different conditions.
+The line below this paragraph, {{ABSTRACT_PUBMED_12832766}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12832766 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12832766}}
 ==About this Structure==
@@ Line 36: / Line 40: @@
 [[Category: Psi]]
 [[Category: Structural genomic]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:27:43 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:52:12 2008''